Abstract
At the time when the first edition of this book was written, two sets of methods were available for the investigation of cutis structure: microscopical methods and chemical methods. Both areas of investigation were sharply limited by the size of the investigated objects. Only structures larger than 0.2 μ (= 2000 Å) could be investigated under the microscope. Only structures smaller than 0.005 μ (= 50 Å) could be successfully studied by direct chemical analysis. The methods of classical organic chemistry, created for the analysis of substances of small molecular weight, could be applied to splitting products of macromolecular substances, but gave only indirect clues when applied to the macromolecules themselves.—Very little was known about the biological structures which are too small to be visible microscopically and too complicated to give easily interpretable results when analyzed with the usual methods of analytical chemistry.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Bibliography
Adair, G. S., H. F. Davis and S. M. Partridge: A soluble protein derived from elastin. Nature (Lond.) 167, 605 (1951).
Adams, J. B.: Identification of isomeric chondroitinsulfates. Nature (Lond.) 186, 555 (1960).
Adlersberg, D., C. I. Wang and L. Stauss: The role of the ground substance in atherogenesis. J. Mt Sinai Hosp. 24, 655 (1957).
Aizawa, I.: Biochemical studies on carbohydrates. Itinsulfuric acids in pig skin. Tôhoku J. exp. Med. 65, 375 (1957).
Biochemical studies on carbohydrates. On the mode of union between itinsulfuric acids and proteins in pig skin Tôhoku J. exp. Med. 65, 383 (1957).
Aldrich, B. I.: Effects of the hyaluronic acid complex on the distribution of ions. Biochem. J. 70, 236 (1958).
Alekseeva, A. S.: Changes in the activity of the enzyme system which catalyzes the synthesis and hydrolysis of elastic vessel fibers in experimental atherosclerosis. Ateroskleroz i Koronar. Nedostatochnost. Sbornik 1956, 137.
Allgöwer, M., and L. Hulliger: Origin of fibroblasts from mononuclear blood cells: a study on in vitro formation of the collagen precursor, hydroxyproline, in buffy coat cultures. Surgery 47, 603 (1960).
Altshuler, C. H., and D. M. Angevine: Histochemical studies on the pathogenesis of fibrinoid. Amer. J. Path. 25, 1061 (1949).
Acid mucopolysaccharides in degenerative disease of connective tissue, with special reference to serous inflammation. Amer. J. Path. 27, 141 (1951).
Ambrose, E. J., and A. Elliott: Infrared spectra and structure of fibrous proteins. Proc. roy. Soc. A 206, 206 (1951).
Ames, W. M.: The conversion of collagen to gelatin and their molecular structure. J. Sci. Food Agric. 3, 454 (1952 a).
Titration curves of two types of gelatin. J. Sci. Food Agric. 3, 579 (1952b).
Aniprino, R.: Distribution of sodium S35 sulfate in early chick embryos. Experientia (Basel) 11, 19 (1955).
Anderson, L., A. M. Landel and D. F. Diedrich: The galactose-glucose conversion in isotopic water. Biochim. biophys. Acta 22, 573 (1956).
Andreeva, N. S., N. G. Esipova and M. I. Millioxova: On peculiarities in the structure of collagen. Kristallografiya 2, 470 (1957).
Arbuzov, G. A.: Isoelectric point of collagen. Nauch. Trudy Moskov. Tekhnol. Inst. Legkoi Prom. 4, 70 (1954).
Arvy, L., and C. Sors: Histochemical study of amyloid. Acta histochem. (Jena) 66, 77 (1958).
Asboe-Hansen, G.: The origin of synovial mucin. Ehrlich’s mast cell—a secretory element of the connective tissue. Amer. J. Rheumat. Dis. 9, 149 (1950 a).
The variability in the hyaluronic acid content of the dermal connective tissue under the influence of thyroid hormone. Acta derm.-venereol. (Stockh.) 30, 221 (1950b).
Autoradiography of mast cells in experimental skin tumors of mice injected with radioactive sulfur (S35). Cancer (Philad.) 13, 587 (1953).
Autoradiographic evidence of cortisone action on mast cells in experimental skin tumors. Cancer Res. 14, 94 (1954).
Asboe-Hansen, G., and D. Glick: Influence of various agents on mast cells isolated from rat peritoneal fluid. Proc. Soc. exp. Biol. (N.Y.) 98, 458 (1958).
Asboe-Hansen, G., and K. Iversen: Influence of thyrotropic hormone on connective tissue. Pathogenetic significance of mucopolysaccharides in experimental exophthalmos. Acta endocr. (Kbh.) 8, 90 (1951).
Astbury, W. T.: The molecular structure of the fibers of the collagen group. J. Intern. Soc. Leather Trades Chem. 24, 69 (1940).
Astbury, W. T., and F. O. Bell: Molecular structure of the collagen fibers. Nature (Lond.) 145, 421 (1940).
Bachman, C., S. B. Cor.r.TP and H. S.LYE: Further studies of sex skin reactions in Ma-caca mulatta. Proc. Soc. exp. Biol. (N.Y.) 33, 549 (1936).
Bagdy, D., and I. Banga: Extraction and purification of elastase from dried pancreas. Acta physiol. Acad. Sci. hung. 11, 371 (1957).
Adsorption of elastase by means of synthetic sodium aluminum silicate. Experientia (Basel) 14, 64 (1958).
Bagdy, D., P. Tolnay, J. Borsy and K. Kov.Ics: Chemical, biological and pharmacological properties of elastase, and its therapeutic application. Mag. Tudomanyos Akad. Biol. és Orvosi Tudomanyok Osztâlyânak Közleményei 11, 277 (1960).
Bairati, A., e F. Massabi: Richerche sui fattori the influenzano la colorazione argentica delle strutture fibrose del connettivo. III. Connettivo reticolato. Boll. Soc. ital. Biol. sper. 29, 1 (1953).
Bairati, A., e M. Paterno: Osservazioni sulla solubilita del tessuto fibroso e del collagene in soluzioni concentrate di urea. Boll. Soc. ital. Biol. sper. 30, 1079 (1954).
Bakeland, E.: The in vivo study of mast cells. Ann. histochim. 3, 179 (1958).
Baker, B. L., D. J. Ingle, C. H. Li and H. M. Evans: Growth inhibition in the skin induced by parenteral administration of adrenocorticotropin. Anat. Rec. 102, 313 (1948).
Baker, B. L., and W. L. Whitaker: Interference with wound healing by the local action of adrenocortical steroids. Endocrinology 46, 544 (1950).
Baker, E. M., H. E. Sauberlich and S. J. Wolfskill Metabolism of C14–6-D-glucuronolactone and C14–6-D-glucuronic acid in man. Fed. Proc. 20, 85 (1961).
Balacz, E. A., and L. Sundblad: Viscosity of hyaluronic acid solutions containing proteins. Acta Soc. Med. upsalien. 64, 137 (1959).
Balacz, E. A., and J. A. Szirmai: Dye binding and mucosacch. content of conn. tissue. J. Histochem. Cytochem. 6, 416 (1958).
Bal, J., and I. Banda: Elastase and elastase inhibitor. Nature (Loud.) 164, 491 (1949).
The elastolytic activity of pancreatic extracts. Biochem. J. 46, 384 (1950).
Change in the elastase content of the human pancreas in relation to arteriosclerosis. Acta physiol. stand. 4, 187 (1953).
The swelling of collagen and its prevention by adenosinetriphosphate (ATP). Mag. Akad. Biol. Orvosi Tudomdnyok Osztâlyanak Közleményei 9, 75 (1958).
Bala, J., I. Banca and D. Szabó: Examination of the structure of collagen tissue. Mag. Tudomanyos Akad. Biol. és Orvosi Tudomanyok Osztalyanak Köz1e-ménvei 7, 385 (1956).
Metacollagen as apparent elastin. Mag. Tudomanyos Akad. Biol. Orvosi Tudomanyok Osztalyanak Közleményei 8, 229 (1957).
Balo, J., D. Szab and I. Banca: The action of collagen mucoproteinase on the neutral mucopolysaccharides of collagen fibers. Acta histochem. (Jena) 9, 69 (1960).
Bandlrski. R. S., L. G. Wilson and C. L. Squires: The mechanism of “active sulfate” formation. J. Amer. chem. Soc. 78, 6408 (1956).
Banfield, W. G.: The solubility and swelling of collagen in dilute acid with age variations in man. Anat. Rec. 114, 157 (1952).
Width and length of collagen fibrils during the development of human skin, in granulation tissue and in the skin of adult animals. J. Geront. 10, 13 (1955).
Effect of growth hormone on acetic acid-extractable collagen of hamster skin. Proc. Soc. exp. Biol. (N.Y.) 97, 309 (1958).
Banca, I.: Eaastolytic enzyme. Abstr. Communs. 1 st. Internat. Congr. Biochem. 122 (1949).
The enzymic break-down of the structure proteins of the aorta. II. Congr. Intern. de Biochim. (Résumés des Communications) p. 269, Paris, 1952.
Thermal contraction of collagen and its dissolution with elastase. Nature (Loud.) 172, 1099 (1953).
The effect of weak organic acids on the rat tail collagen fiber of young and old animals. Gerontologia (Basel) 1, 325 (1957).
Banca, I., and Baló: Elastomucoproteinase and collagenmucoproteinase, the mucolytic enzymes of the pancreas. Nature (Lond.) 178, 310 (1956).
The effect of adenosinetriphosphate and of acid swelling on collagen. Biokhimiya 22, 60 (1957).
Isolation of neutral heteropolysaccharide containing mucoprotein from bovine achilles tendon with the aid of collagen mucoproteinase. Biochem. J. 74, 388 (1960a).
Elasticity-increasing property of elastomucoproteinase. Biochim. biophys. Acta 40, 367 (1960b).
Banda, I., J. Bale and D. Szabo: Procollagen as a component of collagen fibers. Acta physiol. Acad. Sci. hung. 9, 61 (1956a).
Metacollagen as the apparent elastin. J. Geront. 11, 242 (1956b).
The structure, aging, and rejuvenation of collagen fibers. Experientia (Basel) Suppl. No 4, 28 (1956 c).
Bangle jr., R., and W. C. Alford: The chemical basis of the periodic acid-Schiff reaction of collagen fibers with reference to periodate consumption by collagen and by insulin. J. Histochem. Cytochem. 2, 62 (1954).
Baptist, V. H., and H. B. Bull: Determination of the terminal carboxyl residues of peptides and of proteins. J. Amer. chem. Soc. 75, 1727 (1953).
Barer, G. R.: Quantitative measurements on spreading phenomena in skin. Brit. J. Pharmacol. 9, 346 (1954).
Barker, S. A., A. B. Foster, I. R. Siddiqui and M. Stacey: Uronic acid determination. Talanta 1, 216 (1958).
Barrollier, J . , and E. Watzke: Bemerkungen zur Färbung mit dem Perjodsäure-Schiff’s Reagens. Naturwissenschaften 43 , 398 (1956).
Baxter, H., C. Schiller, J. Whiteside and R. E. Straith: The influence of cortisone on skin and wound healing in experimental animals. Plast. reconstr. Surg. 7, 24 (1951).
Bazin, S., and A. Delaunay: Collagen. X. Modifications produced in vitro combinations of collagen-mucopolysaccharides. Ann. Inst. Pasteur 92, 459 (1957).
The influence exerted upon collagen-mucopolysaccharide combinations by several polypeptides, a function of their neutral or basic character. C. R. Acad. Sci. (Paris) 246, 2190 (1958).
Bazin, S., A. Delaunay and N. Briquelet: Collagen. XI. Quantitative examination of in vitro combinations of collagen A-mucopolvsaccharide acid. Ann. Inst. Pasteur 93, 624 (1957).
Collagen. XIII. Effect of different polypeptides, especially extracts of inflammatory granulomas, on collagen mucopolysaccharide combinations in vitro. Ann. Inst. Pasteur 95, 520 (1958).
Bear, R. S.: X-ray diffraction studies on protein fibers. I. The large fiber-axis period of collagen. J. Amer. chem. Soc. 66, 1297 (1944).
Becker, C. E., and H. G. Day: Utilization of glucose and the synthesis of glucosamine in the rat. J. biol. Chem. 201, 795 (1953).
Beek, jr., J.: Carbohydrate in collagen. J. Amer. chem. Soc. 63, 1483 (1941).
Beloff, A., and R. A. Peters: Observations upon thermal burns; influence of moderate temperature burns upon proteinase of skin. J. Physiol. (Lond.) 103, 461 (1945).
Benassi, G.: Aumento del mucopolisaccaridi tessulati nel girino trattato con-4-metil-2-tiouracile. Boll. Soc. ital. Biol. sper. 31, 659 (1955).
Benassi, G., e G. Prodi: Sulla determinazione delle esosamine totali nei tessuti: richerche sul connettivo sottocutaneo e sul derma di ratto albino normale. G. Biochim. 2, 424 (1953).
Benassi, G., and F. Tinacci: Excretion of mucopolysaccharides in urine. Lancet 1953, I , 952.
Bennhold, H.: Über die Ausscheidung intravenös einverleibten Kongorotes bei den verschiedensten Erkrankungen, insbesondere bei Amyloidosen.
Dtsch. Arch. klin. Med. 142, 32 (1923).
Berenson, G. S.: Production of acid mucopolysaccharides by fibroblasts in synthetic medium. Fed. Proc. 17, 741 (1958).
Berenson, G. S., and E. R. Dalferes jr.: Identification of acid mucopolysaccharides from granulation tissue in rats. Brit. J. exp. Path. 41, 422 (1960).
Berenson, G. S., M. Lumpkin and V. G. Shipp: The time-course production of acid mucopolysaccharides by fibroblasts in a synthetic medium. Anat. Rec. 132, 585 (1958).
Berenson, G. S., S. Roseman and A. Dorfman: Chromatographic method for the separation of acid mucopolysaccharides. Biochim. biophys. Acta 17, 75 (1955).
Bergfeld, W., and J. Kapfhammer Belastungsversuche mit Glucossamin bei Mensch und Tieren. Dtsch. Z. Verdau.- u. Stoffwechselkr. 8, 113 (1944).
Bergmann, W., and W. H. Stein: A new principle for the determination of amino acids and its application to collagen and gelatin. J. biol. Chem. 128, 217 (1939).
Betheil, J. J., and P. M. Gallop: Guanidination of lysine hydroxylysine in ichthyocol. Biochim. biophys. Acta 45, 598 (1960).
Beveridge, J. M. R., and C. C. Limes Amino acids of isinglass. J. biol. Chem. 155, 547 (1944).
Bidwell, E., W. E. Van Heyningen and P. A. Charlwood: The biochemistry of the gas gangrene toxins. V. The kappa toxin (collagenase) of Cl. welchii. Biochem. J. 42, 140 (1948).
Bjorksten, J., F. A. Andrews, J. Bailey and B. Trenk: Fundamentals of aging: Immobilization of proteins in whole-body irradiated white rats. J. Amer. Geriat. Soc. 8, 37 (1960).
Blumberg, B. S., G. Oster and K. Meyer: Changes in the physical characteristics of ground substance with alterations in the sodium chloride concentration. J. clin. Invest. 39, 1456 (1955).
Boas, N. F.: Method for the determination of hexosamines in tissues. J. biol. Chem. 204, 553 (1953).
Distribution of hexosamine in electrophoretically separated extracts of rat connective tissue. Arch. Biochem. 57, 367 (1955).
Effects of hormones on connective tissue and mucoproteins. Ann. N.Y. Acad. Sci. 72, 1045 (1959).
Boas, N. F., and J. B. Foley: Regulation of connective tissue levels by the anterior pituitary and thyroid glands. Proc. Soc. exp. Biol. (N.Y.) 87, 89 (1954).
Boas, N. F., and M. Reiner: Effect of ACTH and cortisone on serum hexosamine and gamma globulin levels in acute disseminated lupus erythematosus. J. clin. Endocr. 11, 890 (1951).
Boas, N. F., and L. F. Softer: The effect of adrenocorticotropic hormone and cortisone on the serum hexosamine level in acute disseminated lupus erythematosus. J. clin. Endocr. 11, 39 (1951).
Boedtker, H., and P. Doty: The native and denatured states of soluble collagen. J. Amer. Chem. Soc. 78, 4267 (1956).
Borvn, A., R. Vendrely and C. Vendrely: Desoxyribonucleic acid as the site of hereditary characters in the cell nucleus: evidence based on analyses. C. R. Acad. Sci. (Paris) 226, 1061 (1948).
Bollet, A. J., J. F. Goodwin and A. K. Brown: Metabolism of mucopolysaccharides in connective tissues. J. clin. Invest. 38, 451 (1959).
Bollet, A. J., J. F. Goodwin, WM. F. Simpson and D. V. Anderson: Mucopolysaccharide, protein, and deoxyribonucleic acid concentration of granulation tissue induced by polyvinyl sponges. Proc. Soc. exp. Biol. (N.Y.) 99, 418 (1958).
Bollet, A. J., and A. Shuster: Metabolism of mucopolysaccharides in connective tissue. II. Synthesis of glucosamine 6-phosphate. J. clin. Invest. 39, 1114 (1960).
Bonelli, M.: Protein fractions and blood serum mucoproteins in pemphigus herpetiform dermatitis, and herpes gestationis. G. ital. Derm. Sif. 97, 43 (1956).
Bonelli, M., and G. Armuzzi: Protein and glyco and lipoprotein alterations of serum after burns. G. ital. Derm. Sif. 99, 291 (1958).
Bonifaz, J. I.: Determination of mucoproteins in the burned child. Rev. Hosp. Nino (Lima) 22, 103 (1960).
Bonomo, E., e M. Chirico: Sul comportamento dei glicoproteidi serici nello scorbuto sperimentale della cavia. Acta vitamin. (Milano) 8, 174 (1954).
Boström, H., and S. Gar-Dell: Uptake of sulphates in mucopolysaccharides esterfield with sulphuric acid in the skin of adult rats after intraperitoneal injection of S35 labelled sodium sulphate. Acta Chem. scand. 7, 216 (1953).
Boström, H., L. Rodénand A. Vestermark: Glutamine as an accelerator of chondroitinsulfate synthesis. Nature (Lond.) 176, 601 (1955).
Boucek, R. J., N. L. Noble, Y. T. Kao and H. R. Elden: The effects of age sex and race upon the acetic acid soluble fractions of collagen (human biopsy connective tissue). J. Geront. 13, 1 (1958).
Boucek, R. J., N. L. Noble and J. E. Woessner jr.: Properties of fibroblasts: Properties of fibroblasts. “Connective tissue, thrombosis and atherosclerosis.” Edit. IRVINE H. PAGE, p. 193.: Academic Press 1959.
Bowen, T. J.: Physical studies on a soluble protein obtained by the degradation of elastin with urea. Biochem. J. 55, 766 (1953).
Bowes, J. H.: Some observations on the amino acid distribution of collagen, elastin, and reticular tissue from different sources. Biochem. J. 45, 281 (1949).
Composition of skincollagen and the effect of alkalis on collagen. Research 4, 155 (1951).
Bowes, J. H., R. G. Elliott and J. A. Moss: Collagen and acid-soluble collagen. Biochem. J. 61, 143 (1955).
The composition of some protein fractions extracted from calf skin. Biochem. J. 63, 1 P (1956).
Collagen and the more soluble constituents of skin. J. Soc. Leather Trades ’ Chemists 41, 249 (1957).
Bowes, J. H., and R. H. Kenten• Amino caid composition and titration curve of collagen. Biochem. J. 43 , 358 (1948 a).
The effect of alkalis on collagen. Biochem. J. 43, 365 (1948b).
Some observations on the amino acid distribution of collagen, elastin, and reticular tissue from different sources. Biochem. J. 45, 281 (1949).
Bowes, J. H., and J. A. Moss: The reaction of Fluorodinitrobenzene with the and e-amino groups of collagen. Biochem. J. 55, 735 (1953).
Bracco, M., and P. C. Curti: New histochemical reaction for detecting sulfomucins.Biol. lat. (Milano) 6, 412 (1953).
Braun-Falco, O., u. R. Geimer: Die Wirkung von Hyaluronidase und Heparin auf experimentelle Hautblasen. Arch. Derm. Syph. (Berl.) 197, 42 (1953).
Braun-Falco, O., u. G. Weber: Die Wirkung der Hyaluronidase auf Entzündungen der Haut. Hautarzt 4, 164 (1953).
Braun-Falco, O., and K. Salfeld: Biochemistry and histochemistry of senile elastosis. Derm. Wschr. 135, 374 (1957).
Bull. Soc. franç. Derm. Syph. 64, 586 (1957).
Braun-Falco, O., G. Weber and G. Thaesler: Verhalten der proteingebundenen Serum-polysaccharide in Dermatosen. I. Methode. Arch. Derm. Syph. (Berl.) 198, 584 (1954).
Brewer, D. B.: Myxoedema: an autopsy report with histochemical observations on the nature of mucoid infiltrations. J. Path. Bact. 63, 503 (1951).
Brown, D. H.: The phosphorylation of D(+)-glucosamine by crystalline yeast hexokinase. Biochim. biophys. Acta 7, 487 (1951).
Action of phosphoglucomutase on d-glucosamine-6-phosphate. J. biol. Chem. 204, 877 (1953).
Tissue storage of mucopolysaccharides in Hurler-Pfaundler’s disease. Proc. nat. Acad. Sci. (Wash.) 43, 783 (1957).
Brown. P. C., and R. Consden: Variation with age of shrinkage temperature of human collagen. Nature (Lond.) 181, 349 (1958).
Brown, P. C., R. Consden and L. E. Glynn: Observation on the shrink temperature of collagen and its variation with age and disease. Ann. rheum. Dis. 17, 196 (1958).
Bunting, H., and R. F. White: Histochemical studies of skin wounds in normal and in scorbutis guinea pigs. Arch. Path. (Chicago) 49, 590 (1950).
Burton, D., D.A. Hall, M. K. Keech, R. Reed, H. SA%L, R. E. TUNBRIDGE and M. J. WOOD: Apparent transformation of collagen fibrils into elastin. Nature (Lond.) 176, 966 (1955).
Butt-Urine, U.. and E. Pretolani: Method for the evaluation of the elastolytic activity of pancreatic extract. Boll. Soc. ital. Biol. sper. 34 , 116 (1958).
Bychxov, S. M.: Complex formation of hyaluronic and chondroitinsulfuric acids with procollagen. Dokl. Akad. Nauk SSSR. 75. 83 (1950).
Bychkov, S. M., and V. A. Fomina: Reactions between chondromucoid and procollagen. Vop. med. Khim 4, 59 (1958).
Cabib, E . , L. F. Leloir and C. E. Cardini: Uridine diphosphate acetylglucosamine. J. biol. them. 103 , 1055 (1953).
Caccialanza, O., e M . Bonelli• Valutazione delle muco- proteine del siero di sangue in varie dermatosi. G. ital. Derm. Sif. 5, 1 (1954) .
Calkins, E., A. S. Cohen and B. Larsen: Amyloidosis: preliminary clinical, chemical and experimental observations. Ann. N.Y. Acad. Sci. 86, 1033 (1960).
Caputo, A.: Comportamento elettroforetico di estratti di sarcoma di Rous sottoposti ad ultracentrifugazeione. Tumori 91, 194 (1955).
Carnes, W. H., and B. R. Forker: Metachromasia of amyloid deposits. J. Histochem. Cytochem. 2, 469 (1954).
Carstensen, H . , and H . Linderholm: The effect of adrenocorticotropic hormone on dermal spread. Acta endocr. (Kbh.) 9 , 6 (1952).
Cassel, J. M.: Degradation of collagen by heat. J. Amer. Leather Chemists ’ Ass. 53, 507 (1958).
Castellani, A.: Photodynamic depolymerization of hyaluronic acid by hematoporphyrin. G. biochem. ital. 3, 19 (1954).
Castellani, A., B. DE Bernard and V. Zambotti: Glucuronic acid formation in epiphyseal cartilage homogenate. Nature (Lond.) 180, 859 (1957).
Castellani, A., G. Ferri, L. Bolognani and V. Graziano: Presence of sialic acid in connective tissue. Nature (Lond.) 185, 37 (1959).
Castor, C. W., and B. L. Baker: The local action of adrenocortical steroids on epidermis and connective tissue of the skin. Endocrinology 47, 234 (1950).
Catchpole, H. R.: Serum and tissue glycoproteins in mice bearing transplantable tumors. Proc. Soc. exp. Biol. (N.Y.) 75, 221 (1950).
Cawley, E. P., C. H. Lupton jr., C. E. Wheeler and J. F. Mcmanus: Examination of normal and myxedematous skin: use of Mowry’s alcian blue-periodate acid-Schiff technique. A.M.A. Arch. Derm. 76, 637 (1957).
Chain, E., and E. S. Duthie: Identity of hyaluronidase and spreading factor. Brit. J. exp. Path. 21, 324 (1940).
Chou, T. C., and M. Soodak: The acetylation of d-glucosamine by pigeon liver extracts. J. biol. Chem. 196, 105 (1951).
Christensen, H. E., R. Rask-Nielsen and J. Clausen: Biochemical changes in experimental amyloidosis.
I. Morphological and histochemical studies on the tissues of mice in experimental amyloidosis. Protides. Biol. Fluids, Proc. 7th Colloq. Bruges, Belg., p. 184, 1959.
Chvapil, M., and B. Vmuchalovii: Biological significance of peptides containing hydroxyproline during the development of carrageenin granuloma. Nature (Lond.) 186, 806 (1960).
Chvapil, M., and R. Zahradník: Fibroplasia. VIII. Changes in the rate of hydrolysis of connective tissue proteins during age. Phvsiol. Bohemoslov. 7, 227 (1958).
Cifonelli, J. A., and L. Dorfman: Properties of heparin monosulfate (Heparitin monosulfate). J. biol. Chem. 235, 3283 (1960).
Cifonelli, J. A., J. Ludowieg and A. Dorfman: Chemistry of ß-heparin (chondroitinsulfuric acid B). J. biol. Chem. 233, 541 (1958).
Clausen, J., H. E. Christensen and R. Rash Nielson: III. Immunochemical investigations on serums and urines from mice with experimental amyloidosis. Protides. Biol. Fluids. Proc. 7th. Colloq. Bruges, Belg, p. 196, 1960.
Clerici, E., and B. Pernis: The carbohydrate content of pathological hyaline tissues. Acta histochem. (Jena) 6, 174 (1958).
Cohen, H., H . Megel and W. Kleinberg: Pancreatic elastase. I. Observations on cellular courte and endocrine influence. Proc. Soc. exp. Biol. (N.Y.) 97, 8 (1958).
Consden, R.,L. E. Glynn and W. M. Stanier: A chemical examination of connective tissue in rheumatic fever. Biochem. J. 55, 248 (1953).
Cooper, D. R.: Formation of fibrils from extracts of bovine hide. Biochim. biophys. Acta 26, 330 (1957).
Cooper, D. R., and P. Johnson: Formation of fibrils from extracts of skin. Biochim. biophys. Acta 20, 411 (1956).
Cornbleet, T.: Cutaneous carbohydrates. I. The normal skin. Arch. Derm. Syph. (Chicago) 41, 193 (1940).
Courts, A.: The N-terminal amino acid residues of gelatin. I. Intact gelatins. Biochem. J. 58, 70 (1954 a).
II. Thermal degradation. Biochem. J. 58, 14 (1954b).
III. Enzymic degradation. Biochem. J. 59, 382 (1955).
Cowan, P. M., and S. Mcgavin: The structure of poly-L-proline. Congr. intern. biochim., Resumes cornmuns., 3e Congr. Biochem. Brussels, p. 18, 1955.
Cowan, P. M., S. Mcgavin and A. C. T. North: The polypeptide chain configuration of collagen. Nature (Lond.) 176, 1062 (1955).
Crewther, W. G., and L. M. Dowling: The thermal shrinkage of collagen in solutions of electrolytes. J. physic. Chem. 62, 678 (1958).
Crick, F. H. C.: A structure for collagen. J. them. Physics 22, 347 (1954).
Crick, F. H. C., and A. Rich: Structure of polyglycine. II. Nature (Lond.) 176, 780 (1955).
Csaba, G.: Role of mucopolysaccharides in the growth of tumors. Orv. Szle 100, 1882 (1959).
Curran, R. C., and J. S. Kennedy: The distribution of sulphated mucopolysaccharides in the mouse. J. Path. Bact. 70, 449 (1955).
Danielli, J. F., H. B. Fell and E. Kodicek: Enzymes of healing wounds: effect of different degrees of vitamin C deficiency on phosphate activity in experimental wounds in guinea pigs. Brit. J. exp. Path. 26, 367 (1945).
Danishefsky, I., and F. J. Borrelli: Studies made with radioactive heparin in humans. Angiology 11, 40 (1960).
Danishefsky, I., H. B. Eiber and J. J. Carr: Investigations on the chemistry of heparin. I. Desulfation and acetylation. Arch. Biochem. 90, 114 (1960).
Davidson, E. A., H. J. Blumenthal and S. Roseman: Studies on glucosamine-6-phosphate N-acetylase. Bact. Proc. 108 (1956).
J. biol. Chem. 226, 125 (1957).
Davidson, E. A., and K. Meyer: Structural studies on chondroitinsulfuric acid. The glucuronidic linkage. J. Amer. them. Soc. 77, 4796 (1955).
Davidson, E. A., and J. G. Riley: Chondroitinsulfate B metabolism. Biochim. biophys. Acta 42, 566 (1960).
Davidson, E. A., W. Small and P. Perchemlides• Hormonal control of mucopolysaccharide metabolism. Fed. Proc. 20, 162 (1961).
Davidson, E. A., W. Small, P. Perchemlides and W. Baxley: Age-dependent metabolism of connective-tissue polysaccharides. Biochim. biophys. Acta 46, 189 (1961).
Deasy, C. L.: Use of the thiohydantoin method for the determination of the terminal carboxyl amino acids of collagen. J. Amer. Leather Chemists ’ Ass. 51, 584 (1956).
DE Bellis, R., I. Mandl, J. D. Maclennan and E. L. Howes: Separation of proteolytic enzymes of Clostridium histolyticium. Nature (Lond.) 174, 1191 (1954).
Degos, R., and F. Cottenot: Role of mast cells in the metabolism of connective tissues. Bull. Soc. franç. Derm. Syph. 64, 548 (1958).
Delaunay, A., and S. Bazin: Collagen. VII. A.tion of chondroitinsulfuric acid on solutions of collagen A. Bull. Ass. Dipl. Microbiol. Nancy 62, 5 (1956).
Lesliaisons collagène-mucopolysaccharides et leur importance en biologie. Bull. Soc. franç. Derm. Syph. 64, 534 (1957).
DEL Conte, E., J. D. Sala and M. Stux: Action of thyroidectomy, thiourea, and iodine on the labrocytes and acid mucopolysaccharides of the skin of the rat. Rev. Soc. argent. Biol. 30, 265 (1954).
Effect of thyroidectomy, thiourea, and iodine on the labrocytes and acid mucopolysaccharides of the skin of the rat. Acta endocr. (Kbh.) 20, 343 (1955).
Delmotte, A.: Intervention of bacterial and serum factors on the ground substance of skin. Bull. Soc. franç. Derm. Syph. 64, 578 (1957).
DE Moxcuit, M., and L. Robert: Determination of uronic acid in tissue extracts. Ann. Biol. clin. 17, 475 (1959).
DE Nicola, P . , S. Altieri and G. M. Mazzetti: Thromboelastographic and bloodcoagulative study of some heparinlike synthetic substances. Haematologica 41 , 149 (1956).
Denisova, A. A., and A. L. Zaides • Amino acid composition of collagen Fractions From An Guinea Pig. Dokl. Akad. Nauk Sssr. 114, 1287 (1957).
Denisova, A. A., A L Zaides and A. N. Mikhailov • Quantitative chromatographic analysis in laboratory practice in leather production. Legkaya Prom. 17, No 9, 23 (1957).
Dick, J. C.: Observations on the elastic tissue of the skin. J. Anat. (Lend.) 81, 201 (1947).
DI Ferrante, N.: Turbidimetric measurement of acid mucopolysaccharides and hyaluronidase activity. J. biol. Chem. 220, 303 (1956).
DI Ferrante, N., W. C. Robbins and C. Rich: Urinary excretion of acid mucopolysaccharides by patients with lupus erythematosus. J. Lab. clin. Med. 50, 897 (1957).
Dische, Z.: A new specific color reaction of hexuronic acids. J. biol. Chem. 167, 189 (1947).
Dodds, E. C., and J. D. Robertson: The clinical application of dinitro-o-cresol. II. A study of myxoedema. Lancet 1933 II, 1197.
Dorfman, A., and A. E. Lorincz: Occurrence of urinary acid mucopolysaccharides in the Hurler syndrome. Proc. nat. Acad. Sci. (Wash.) 43, 443 (1957).
Dorfman, A., A. Markovitz and J. A. Clfonelli• Metabolism of hyaluronic acid and chondroitinsulfuric acids. Fed. Proc. 17, 1093 (1958).
Dorfman, A., S. Roseman, F. E. Moses, J. Ludowieg and M. Mayeda: The biosynthesis of hyaluronic by group A streptococcus. III. Origin of the N-acetylglucosamine moiety. J. biol. Chem. 212, 583 (1955).
Dunphy, J. E., and K. N. Udupa: Chemical and histochemical sequences in the normal healing of wounds. NewEngl. J. Med. 253, 847 (1955).
Duran-Reynals, F.: The effect of extracts of certain organs from normal and immunized animals on the infecting power of vaccine virus. J. exp. Med. 50, 327 (1929).
Tissue permeability and the spreading factors in infection; a contribution to the host: parasite problem. Bact. Rev. 6, 197 (1942).
Duran-Reynals, F., H. Bunting and C. Van Wagenen: Studies on the sex skin of Macaca mulatta. Ann. N. Y. Acad. Sci. 52, 1006 (1950).
Eastoe, J . E.: The amino acid composition of mammalian collagen and gelatin. Biochem. J. 61 , 589 (1955).
Amino-acid composition of fish collagen and gelatin. Biochem. J. 65, 363 (1957).
Eastoe, J. E., J. E. Long and A. L. D. Willan: The amide nitrogen content of gelatins. Biochem. J. 78, 51 (1961).
Eiber, H. B., I. Danishefsky and F. J. Borrelli: Studies made with radioactive heparin in humans. Angiology 11, 40 (1960).
Einbinden, J., and M. Schubert: Binding of mucopolysaccharides and dyes by collagen. J. biol. Chem. 188, 335 (1951).
Ejiri, I Studien über die Histologie der menschlichen Haut. III. Mitteilung: LYber die regionären und Altersunterschiede der verschiedenen Hautelemente mit besonderer Berücksichtigung der Altersveränderung der elastischen Fasern. Jap. J. Derm. 41, 8 (1937).
Elson, L. A., and W. T. J. Morgan: A colorimetric method for the determination of glucosamine and chondrosamine. Biochem. J. 27, 1824 (1933).
Elster, S. K.: Effect of ascorbic acid deficiency on collagen content of guinea pig tissues. J. biol. Chem. 186, 105 (1950).
Elster, S. K., and E. I. Lowry: Collagen content of guinea pig tissues. Proc. Soc. exp. Biol. (N.Y.) 75, 127 (1950).
Esipova, N. G.: Type of some hydrogen bonds of collagen. Biofizika 2, 461 (1957).
Eskelund, V.: Mucin staining with Alcian Blue. Acta path. microbiol. stand. 40, 107 (1957).
Faillard, H., and H. Stickl: Der Einfluß neuraminsäurehaltiger Mucoproteide und Glvkolipoide auf das Wachstum epithelialer und mesenchvmaler Zellen in Gewebekulturen. Hoppe-Seylers Z. physiol. Chem. 319, 220 (1960).
Faulkner, P., and J. H. Quastel: Anaerobic deamination of D-glucosamine by bacterial and brain extracts. Nature (Lond.) 177, 1216 (1956).
Fauve, R., A. Delaunay, S. Bazin and M. Henon: The action of a human umbilical cord extract rich in mucopolysaccharides on solutions of collagen A. C. R. A.ad. Sci. (Paris) 242,: 306 (1956).
Fell, H. B., and J. F. Danielli: The enzymes of healing wounds. I. The distribution of alkaline phosphomonoesterase in experimental wounds and burns in the rat. Brit. J. exp. Path. 24, 196 (1943).
Felsiier, Z.: Studies on the adherence of the epidermis to the corium. J. invest. Derm. 8, 35 (1947).
Fessler, I. J. H.: Properties of neutral-salt soluble collagen. Biochem. J. 76, 452 (1960).
G. Fischer, Chr. Landschtitz, G. Ehrensvard, M. Rafelson jr. and R. Stjernholm: Amino-acid formation from carbon14 labelled glucose in cultures of fibroblasts from embryonic chicken-heart tissues. Acta physiol. scand. 27, 247 (1953).
Fitch, S. M., M. L. R. Hark-Ness and R. D. Harkness: Extraction of collagen from tissues. Nature (Lond.) 176, 163 (1955).
Fitton-Jackson, S.: Fibrogenesis in vivo and in vitro. Nature and structure of collagen, Disc. by Colloid and Biophys. Comm., Faraday Soc., King’s Coll., London Mar., 1953, p. 140–151, Disc. 152–157.
Fitton-Jackson, S., and R. H. Smith: Biosynthesis of collagen. I . Growth of fowl osteoblasts and the formation of collagen in tissue culture. J. biophys. biochem. Cytol. 3 , 897 (1957 a).
Some aspects of the biosynthesis of collagen. Proc. Conf. Gelatine and Glue Research, 1957 b, p. 54.
Flory, P. J., and E. S. Weaver: Helix-coil transitions in dilute aqueous collagen solutions. J. Amer. them. Soc. 82, 4518 (1960).
Folin, O., H. C. Trimble and L. H. Newman: The distribution and recovery of glucose injected into animals. J. biol. Chem. 75, 263 (1927).
Foot, N. L.: Chemical contrasts between collagenous and reticular tissue. Amer. J. Path. 4, 525 (1928).
Forakeb, A. G., and G. Marino: Estudios bioquimicos en el condrosarcoma. Folia Clin. Int. (Barcelona) 6, 56 (1956).
Fraenkel-Conrat, H. L., and M. Cooper: The use of dyes for the determination of acid and basic groups in proteins. J. biol. Chem. 154, 239 (1944).
Franzblau, C., S. Seifter and P. M. Gallop: Nature of non-dialyzable peptides found after digestion of ichthyocol with collagenase. Fed. Proc. 20, 386 (1961).
Freudenthal, W.: Amyloid in der Haut. Arch. Derm. Syph. (Berl.) 162, 40 (1930).
Fruton, J. S.: On the proteolytic enzymes of animal tissue. V. Peptidases of skin, lung and serum. J. biol. Chem. 166, 721 (1946).
Fr,Jita, K.: Properties of a polysaccharide in chicken sarcoma. Nagoya J. med. Sei. 17, 98 (1954).
Gallop, P. M., S. Seifter, M. Lukin and E. Meilman: Application of the Lossen rearrangement of dinitrophenylhydroxamates to analysis of carboxyl groups in model compounds and gelatin. J. biol. Chem. 235, 2619 (1960).
Gallop, P. M., S. Seifter and E. Meilman: Studies on collagen. I. The partial purification, assay, and mode of activitation of bacterial collagenase. J. biol. Chem. 227, 891 (1957).
Occurrence of esterlike linkages in collagen. Nature (Lond.) 183, 1659 (1959).
Gardell, S., A. H. Gordon and S. Aquist: Electrophoresis of mucopolysaccharides in a slab of Hyflo super-eel. Acta them. scand. 4, 907 (1950).
Gardell, S., F. Heijkenskjöld and A. Rochnorlund: Oxidation of glucosamine and galactosamine with ninhvdrin to arabinose and lyxose and their identification by paper chromatography. Acta chem.’ scand. 4. 970 (1950).
Gazzaniga, M., E. Sabbadini and U. Conti: Behavior of hexosamine substances in experimental Walker’s tumor. Boll. Soc. med.-chic. Pavia 71, 1743 (1957 a).
Behaviorof hexosamine substances in shock from evisceration. II. Hexosamine of liver; kidney, muscle and cutaneous and subcutaneous tissue. Boll. Soc. med.-chir. Pavia 71, 1763 (1957b).
Gedigk, P.: Histochemische Darstellung von Kohlenhydraten. Klin. Wschr. 30, 1052 (1952).
Gedigk, P., and R. Fischer: The adaption of the enzyme activity of histiocytes in functional stages. Klin Wschr. 38, 806 (1960).
Gerber, G. B., G. Gerber and K. I. Altman: Metabolism of tissue proteins.
Turnover of collagen labeled with proline-U-CI’ in young rats. J. biol. Chem. 235, 2653 (1960).
Gerngross, O., and J. R. Katz: X-ray spectrographic investigations of the heat contraction (so-called “Schnurren”) of untanned and formaldehyde-tanned tendons. Kolloidchem. Beih. 23, 368 (1926).
Gersh, I., and H. R. Catchpole: The organization of ground substance and basement membrane and its significance in tissue injury, disease and growth. Amer. J. Anat 85, 457 (1949).
Gilfillan, R. F., A. J. Sbarra and W. A. Bardawil: Serum elastase inhibitor in chronic metabolic and infectious diseases of the aged including temporal arteritis. Fed. Proc. 20, 161 (1961).
Gillman, T., J. Penn, D. Bronks and Rous: Staining reactions of elastic fibers with special references to “Elastic Degenerations” in the human skin. Nature (Lond.) 174, 789 (1954).
Glaser, L., and D. H. Brown: The enzymic synthesis in vitro of hyaluronic acid chains. Proc. nat. Acad. Sci. (Wash.) 41, 253 (1955).
The synthesis of chitin in cell-free extracts of neurospora crassa. J. biol. Chem. 228, 729 (1957).
Glegg, R. E., D. Eidinger and C. P. Leblond: Some carbohydrate components of reticular fibers. Science 118, 614 (1953).
Gold, N. I., and B. S. Gould: Collagen fiber formation and alkaline phosphophatase. Arch. Biochem. 33, 155 (1951).
Gotte, L., and V. Moret: Elastin. II. Mucopolysaccharides in elastin fibers. Atti R. Accad. naz. Lincei, Cl. Sci. fis. mat., natur. 23, 281 (1957).
Products of partial alkaline hydrolysis. Atti R. Accad. naz. Lincei, Cl. Sci. fis. mat., natur. 25, 321 (1958).
Gottschalk, R. G., L. K. Alpert and P. O. Miller Use of large amounts of radioactive sulfur in patients with advanced chondrosarcomas. Cancer Res. 19, 1078 (1959).
Gould, B. S., and J. F. Woessner: Biosynthesis of collagen. The influence of ascorbic acid on the proline, hydroxyproline, glycine, and collagen content of regenerating guinea pig skin. J. biol. Chem. 226, 289 (1957).
Graham, C. E., H. K. Waitkoff and S. W. Hier The amino acid content of some scleroproteins. J. biol. Chem. 177, 529 (1949).
Grant, N. H., and H. E. Albirn: Studies ou the collagenases of clostridium histolyticum. Arch. Biochem. 82, 245 (1959).
Collagen solubilization by mammalian proteinases. Arch. Biochem. 89, 262 (1960).
Grant, H., and K. C. Robbins: Occurrence and activitation of an elastase precursor in pancreas. Proc. Soc. exp. Biol. (N.Y.) 90, 264 (1955).
Porcine elastase and proelastase. Arch. Biochem. 66, 396 (1957).
Grassmann, W.: Collagen. Kolloid.-Z. 77, 205 (1936).
Grassmann, W., H. Endres u. A. STEBER: Esterbindungen im Procollagen. Z. Naturforsch. 9b, 513 (1954).
Grassmann, W., K. Hannig, H. Endres and A. Riedel: Die Aminosäuresequenz im Kollagen. I. Die Position des Prolins and Hydroxyprolins. Hoppe-Seylers Z. physiol. Chem. 306, 123 (1956).
Grassmann, W., and H. Hörmann: Bestimmung der Endgruppen in Collagen und Gelatine. Hoppe-Seylers Z. physiol. Chem. 292, 24 (1953).
Grassmann, W., H. Hörmann u. H. Endres: Untersuchungen über die Anwendbarkeit der Reduktionsmethode zur Bestimmung carboxylendständiger Aminosäuren in Peptiden und Proteinen. Chem. Ber. 88, 102 (1955).
Grassmann, W., H. Hörmann, A. Nordwig and W. Wunsch: Die Spezifität der Collagenase. Hoppe-Seylers Z. physiol. Chem. 316, 287 (1959).
Grassmann, W., U. Hofmann, K. Kuhn, H. Hörmann, H. Endres and K. Wolf: Electron microscopic and chemical studies of the carbohydrate groups of collagen. Connective tissue. Symposium and of the Council for Internat. Organizations of Medical Sciences, p. 157, Paris 1957.
Grassmann, W., and K. Kuhn: The decomposition of collagen and procollagen with sodium periodate and phenyl iodoacetate. Hoppe-Seylers Z. physiol. Chem. 301, 1 (1955).
Grassmann, W., u. H. Suhleich Über den Kohlenhydratgehalt des Kollagens. II. Mitteilung zur Kenntnis des Kollagens. Biochem. Z. 277, 230 (1953).
Graumann, W., and W. Claims: The specificity of the histochemical iron reaction for polysaccharides. Acta histochem. (Jena) 6, 1 (1958).
Graumann, W., and H. Musso: Histological examination of the metachromogenous efficiency of various toluidine blue and Azure A preparations. Histochemie 1, 196 (1959).
Green, J. P., and S. M. Day: Uptake and metabolism of amines by mast cells in culture. Fed. Proc. 20, 136 (1961).
Gregory, J. D., and P. W. Roma /is: Metabolism of sulfur compounds (sulfate metabolism). Ann. Rev. Biochem. 29, 347 (1960).
Gross, J.: Electron microscope studies of sodium hyaluronate. J. biol. Chem. 172, 51 (1948). Structure of elastic tissue as studied with the electron microscope. J. exp. Med. 89, 699 (1949).
A study of certain connective tissue constituents with the electron microscope. Ann. N.Y. Acad. Sci. 52, 964 (1950a).
A study of the aging of collagenous connective tissue of rat skin with the electron microscope. Amer. J. Path. 26, 708 (1950b). — Behavior of collagen units as a model in morphogenesis. J. biophys. biochem. Cytol. 2, Suppl., 261 (1957).
Studies on the fibrogenesis of collagen. Some properties of neutral extracts of connective tissue. Connective Tissue Symposium. Council for Internat. organizations of medical sciences, p. 45, London 1957.
Influence of time on the reversible association between large molecules: the collagen system. Nature (Lond.) 181, 556 (1958 a).
Formation of collagen. III. Time-dependent solubility changes of collagen in vitro. J. exp. Med. 108, 215 (1958b).
IV. Effect of vitamin C deficiency on the neutral salt-extractable collagen of skin. J. exp. Med. 109, 557 (1959).
Gross, J., and B. Dumsha: Elastoidin: a two component member of the collagen class. Biochim. biophys. Acta 28, 268 (1958).
Gross, J., B. Dumsha and N. Glazer: Comparative biochemistry of collagen. Some amino acids and carbohydrates. Biochim. biophys. Acta 30, 293 (1958).
Gross, J., J. H. Highberger and F. O. Schmitt: Some factors involved in the fibrogenesis of collagen. Proc. Soc. exp. Biol. (N.Y.) 80, 462 (1952).
Extraction of collagen from connective tissue by neutral salt solutions. Proc. nat. Acad. Sei. (N.Y.) 41, 1 (1955).
Gross, J., and F. O. Scunitt: The structure of human skin collagen as studied with the electron microscope. J. exp. Med. 8S, 555 (1948).
Grossfeld, H.: Production of hyaluronic acid in tissue culture. The presence of hayluronidase in embryo extract. Exp. Cell Res. 14, 213 (1958).
Grossfeld, H., K. Meyer and G. Golman: Differentiation of fibroblasts in tissue culture, as determined by mucopolysaccharide production. Proc. Soc. exp. Biol. (N.Y.) 8S, 31 (1955).
Gustav Son, K. H.: Hydroxyproline and stability of collagens. Acta them. stand. 8, 1298 (1954).
The chemistry and reactivity of collagen. New York: Academic Press 1956.
Haas, G. M.: Elastic tissue. Arch. Path. (Chicago) 27, 334 (1939).
Haldi, J., G. Giddings and W. Wynn: Dietary control of the water content of the skin of the albino rat. Amer. J. Physiol. 135, 392 (194.2). Hall, C. E., and P. DoTY: A comparison between the dimensions of some macromolecules determined by a electron microscopy and by physico-chemical methods. J. Amer. chem. Soc. S0, 1269 (1958).
Hall, D. A.: Elastin from human tissue and from ox ligament. Nature (Lond.) 168, 513 (1951).
Various elastin preparations as substrates for elastase. 11e Congres Internat. de biochemie, Resumes des Communications, p. 273, Paris 1952.
The reaction between elastase and elastic tissue. Biochem. J. 59, 459 (1955).
Chemical studies on the relation between elastin and collagen. Experientia Suppl. No. 4, 19 (1956).
Collagen and elastin. Effect of age on their relation. Gerontologia 1, 347 (1957).
Hall, D. A., M. K. Keech, R. Reed, H. Sarl, R. E. Tunbridge and M. J. Wood: Collagen and elastin in connective tissue. J. Geront. 10, 388 (1955).
Hall, D. A., and R. Reed: Hydroxyproline and thermal stability of collagen. Nature (Lond.) 180, 243 (1957).
Hall, D. A., R. Reed and R. E. Tunbridge: Structure of elastic tissue. Nature (Lond.) 170, 264 (1952).
Electron microscope studies of elastic tissue. Exp. Cell Res. 8, 35 (1955).
Hammer, D., and J. Marchant: Collagen and other constituents in the skin of normal carcinogen-treated, and castrated mice. Brit. J. Cancer 11, 445 (1957).
Harada, K.: New staining method of polysaccharide sulfate esters. III. Igaku to Seibutsugaku 36, 21 (1955).
Hardesty, M.: The structural basis for the response of the comb of the brown Leghorn fowl to sex hormones. Amer. J. Anat. 47, 277 (1931).
Harkness, R. D., A. M. Marko, H. M. Muir and A. Neuberger: Metabolism of collagen and other proteins of the skin of rabbits. Biochem. J. 56, 558 (1954).
Harpur, R. P., and J. H. Quastel: Phosphorylation of D-glucosamine by brain extracts. Nature (Lond.) 164, 693 (1949).
Har-Rington, W. F.: Effect of neutral salts on the structure of collagen and gelatin. Nature (Lond.) 181 (1958).
Harrington, W. F., and P. H. V. Hippel: Formation and stabilization of the collagen-fold. Arch. Biochem. 92, 100 (1961).
Harrington, W. F., P. H. V. Hippel and E. Mihalyi: Proteolytic enzymes as probes of the secondary structure of fibrous proteins. Biochim. biophys. Acta 32, 303 (1959).
Hashizume, K.: Biochemical studies on carbohydrates CXCVII. Glucidamins in Yoshida Sarcoma. Tôhoku J. exp. Med. 65, 195 (1957).
Hass, O.: Studies of amyloid. II. The isolation of a polysaccharide from amyloid-bearing tissues. Arch. Path. (Chicago) 34, 92 (1942).
Hass, G., R. Huntington and N. Krumdieck: The properties of amyloid deposits occurring in several species under diverse conditions. Arch. Path. (Chicago) 35, 226 (1943).
Hass. G., and R. F. Schultz: Amyloid 1. Methods of isolating amyloid from other tissue elements. Arch. Path. (Chicago) 30, 240 (1940).
Haurowitz, F., M. Tunca, P. Schwerin and V. Göxsu: The action of trypsin on native and denaturated proteins. J. biol. Chem. 157, 621 (1945).
Hausbfrger, F. X., S. W Milstein and R. J. Rutman: The influence of insulin on glucose utilization in adipose and hepatic tissues in vitro. J. biol. Chem. 208, 431 (1954).
Hauss, W. H., G. Junge-Holsing and W. Schultze: Altersbedingte und organbestimmte Unterschiede im Stoffwechsel der Sulfomucopolysaccharide des Bindegewebes. Z. Altensforsch. 14, 259 (1960).
Hayashi, H., T. Ono, K. Udaea and H. Ibuha: Effect of nucleic acid and mucopolvsaccharide on the growth of monocytes in tissue culture. Mie med. J. 4, 133 (1955).
Hayashi, H., K. Tjdaka, T. Funaki and T. Inoue: Acid mucopolysaccharides of ground substance of connective tissue. Mie med. J. 4, 159 (1955).
Hayes, M. A.: The effect of prolonged local treatment with adrenocortical and sex steroids on the intradermal spreading action of hyaluronidase. Endocrinology 52, 646 (1953). — Heathcote, J. G.: Isolation of hydroxvlysine picrate from a gelatin hydrolyzate.
Biochem. J. 42, 305 (1948).
Heckner, F., and R. Strufe: Cytochemischer Nachweis von Polysacchariden mit Natriumperjodat. Klin. Wschr. 34, 326 (1956).
Hedbom, A., and O. Snellman• Isolation and analysis of the large cytoplasmic granules of tissue mast cells. Exp. Cell Res. 9, 148 (1955).
Herbeuval, R., G. Derry and A. Larcan: Study of the effects of adrenocorticotropic hormone and of a somatotropic extract on the cutaneous tissue of the rabbit at the site of injection. Comparative study of the effects of heparin. Ann. Endocr. (Paris) 17, 380 (1956).
Heyns, K., and W. Königsdorf: Proteins and their degradation products. IX. Building block sequence-analysis of collagen. Hoppe-Seylers Z. physiol. Chem. 295, 244 (1953).
Heyns, K., and G. Legler: Proteins and their degradation products. XIII. The carboxyl-terminal and amino-terminal amino acids of gelatin. Hoppe-Seylers Z. physiol. Chem. 306, 165 (1957).
Xvi. The specificity of collagenase from clostridium histolyticum and its use to determine the primary structure of collagen. Hoppe-Seylers Z. physiol. Chem. 115, 288 (1959).
Hieronymi, G.: Vorkommen und Verteilung saurer Muco-polysaccharide in Tumoren. Frankfurt. Z. Path. 65, 409 (1954).
Hill, R., and H. Montgomery: Regional changes and changes caused by age in normal skin. J. invest. Derm. 3, 231 (1940).
Von Hippel, P. H., P. M. Gallop, S. Seifter and R. S. Cunningham • An enzymic examination of the structure of the collagen macromolecule. J. Amer. them. Soc. 82, 2774 (1960).
Hobson, R. P.: On an enzyme from the blow fly larvae (Lucilia sericata) which digests collagen in alkaline solution. Biochem. J. 25, 1458 (1931).
Hgchstein, L. I., J. B. Wolfe and H. L. Nakada • N-Acetylgalactosamine metabolism by proteus vulgaris. Fed. Proc. 18, 247 (1959).
Hodge, A. J., and F. O. Schmitt: Interaction properties of sonically fragmented collagen macromolecules. Proc. nat. Acad. Sci. (Wash.) 44, 418 (1958).
Hörmann, H., and G. Fries: The effect of periodic acid on procollagen. Hoppe-Seylers Z. physiol. Chem. 311, 19 (1958).
Hoffman, P., A. Linker and K. Meyer: Uronic acid of chondroitin sulfate B. Science 124, 1252 (1956).
Acid mucopolysaccharides of connective tissues. Arch. Biochem. 69, 435 (1957).
Chondroitinsulfates. Fed. Proc. 17, 1078 (1958).
Hofmeister, F.: Zur Lehre von der Wirkung der Salze. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 24, 247 (1887/88); 25, 1 (1888/89); 27, 395 (1890); 28, 210 (1890/91).
Holczinger, L.: Influence of fixatives on the periodic acid-Schiff staining of reticular fibers. Acta histochem. (Jena) 3, 19 (1956).
Hotchkiss, R. D.: A microchemical reaction resulting in the staining of polysaccharide structures in fixed preparations. Arch. Biochem. 16, 131 (1948).
Houcx, J. C., and R. A. Jacob: Effect of age on collagen and hexosamine content of rat skin. Proc. Soc. exp. Biol. (N.Y.) 97, 604 (1958).
Some systemic responses to local inflammation. Proc. Soc. exp. Biol. (N.Y.) 98, 655 (1958). Houcx, J. C., and Y. M. PATEL: Pancreatic collagenase. Fed. Proc. 20, 161 (1961).
Hurlbert, R. B., and V. R. Potter: Nucleotide Metabolism. I. The conversion of orotic acid-6-C14 to uridine nucleotides. J. biol. Chem. 209 (1954).
Hvidberg, E., Sv. A. Kvorning, A. Schmidt and J. SCHou: Effect of ultraviolet irradiation on connective tissue. Acta pharmacol. (Kbh.) 15, 365 (1959).
Hvidberg, E., and A. Schmidt • Effect of prolonged cortisone treatment on subcutaneous tissue in mice. Acta pharmacol. (Kbh.) 15, 293 (1959).
Inskip, L. W.: The occurrence of hydroxylysine in proteins. J. Amer. them. Soc. 73, 5463 (1951).
Ishimoto, Y.: Studies on the collagen fiber of skin V. Electronmicroscopy findings on the collagen fiber from the skin area injected with histamine. Tokushima J. exp. Med. 3, 65 (1956). i
Jackson, D. S.: Connective tissue growth stimulated by carageenin. Biochem. J. 65, 277 (1959).
Jackson, D. S., and J. P. Bentley: Significance of the extractable collagen. Cytol. 7, 37 (1960).
Jackson, D. S., and J. H. Fessler • Isolation and properties of a collagen soluble in salt solution at neutral pH. Nature (Lond.) 176, 69 (1955).
Jackson, D. S., D. B. Flickinger and J. Engelbert Dunphy: Biochemical studies of connective tissue repair. Ann. N.Y. Acad. Sci. 86, 943 (1960).
Jackson, D. S., A. A. Leach and S. Jacobs: Amino-acid composition of the collagen fractions of rabbit skin. Biochim biophys. Acta 27, 418 (1958).
Jackson, D. S., and A. Neuberger: The isoionic and isoelectric point of acid-processed gelatin from insoluble and citrate-extracted collagen. Biochim. biophys. Acta 26 (1957).
Jackson, D. S., and G. Williams• Nature of Reticulin. Nature (Lond.) 178, 915–916 (1956).
Jackson, S. F. see: Fitton-Jackson Jacobs, J. L.: A modified technique, for determining protein fractions of animal skin. J. Amer. Leather Chemists ’ Ass. 44, 722–737 (1949).
Jacobson, B.: Uronic acid biosynthesis by skin enzymes. Fed. Proc. 20, 162 (1961).
James, S. P., F. Smith, M. Stacey and L. F. Wiggins: A constitutional synthesis of chondrosamine. Nature (Lond.) 156, 308 (1945).
Jaques, L. B.: Isolation of rat heparin. Canad. J. Biochem. 37, 1183 (1959).
Jeanloz, R. W.: The nomenclature of mucopolysaccharides. Arthritis. Rheumat. 3, 233 (1960).
Jensen, C. E., and F. Carlsen: Hyaluronic acid. VI. An electron microscope study of potassium hyaluronate. Acta them. scand. 8, 1357 (1954).
Jensen, R., O. Snellman and B. Sylven: The inhomogeneity of commercial heparin in preparations from physiochemical point of view. J. biol. Chem. 174, 265 (1948).
Jorpes, J. E., H. Boström and C. V. Mutt: The linkage of the amino group in heparin. J. biol. Chem. 183, 607 (1950).
Jorpes, J. E., and S. Gardell: On heparin monosulfuric acid. J. biol. Chem. 176, 267 (1948).
Jorpes, J. E., H. Holmgren and Wilander: Tuber das Vorkommen von Heparin in den Gefäßwänden and in den Augen. Z. mikr -anat. Forsch. 42, 279 (1937).
Jorpes, J. E., E. Odeblad and H. Boströiu: An autoradiographic study of the uptake of S35 labelled sodium sulphate in the mast cells. Acta haemat. (Basel) 9, 273 (1953).
Es and skin. Bull. Central Leather Research Inst., Madras (India) 4, 343 (1958).
Determination of the carbohydrate constituents of skin proteins. Bull. Central Leather Research Inst., Madras (India) 6, 132 (1959).
Jürgens, R.: Eine neue Reaction of Amyloidkörper. Virchows Arch. path. Anat. 65, 189 (1875).
Jungehülsing, G.: Metabolism of sulfomucopolysaccharides in granulation tissues. Z. Rheumaforsch. 18, 355 (1959).
Kabat, E. A.: A polysaccharide in tumors due to a virus of leucosis and sarcoma of fowls. J. biol. Chem. 130, 143 (1939).
Kalckar, H. M., and E. S. Maxwell: Nature of the enzymic galactose-glucose conversion. Biochim. biophys. Acta 22, 588 (1956).
Kanagy. J. R.: Heats of wetting of collagen, leather and other organic and fibrous materials. J. Amer. Leather Chemists ’ Ass. 49, 646 (1954).
Kanagy, J. R., and J. M. Cassel: Heats of wetting of modified collagen and other materials. J. Amer. Leather Chemists ’ Ass. 52, 248 (1957).
Kao, K. Y. T., and R. J. Boucek: Incorporation and conversion of lysine-2-C“ in rat biopsy connective tissue. Proc. Soc. exp. Biol. (N.Y.) 95, 526 (1958).
In vitro incorporation and hydroxylation of lysine-2-CI’ in rat biopsy-connective tissue. Proc. Soc. exp. Biol. (N.Y.) 98, 530 (1958).
Kao, K. Y. T., D. M. Hilker and T. H. Mogavack: Connective tissue. III. Collagen and hexosamine content of tissues of rats of different ages. Proe. Soc. exp. Biol. (N.Y.) 104, 359 (1960).
Kasai, H.: Acid mucopolysaccharides of the ground substance of connective tissue. III. Mechanism of increased metachromasis in early stage of Arthur-type hypersensitivity. Mie med. J. 9. 275 (1959).
Katz, J. R., and O. Gerngross: Gelatin and collagen. Naturwissenschaften 13, 900 (1925).
Kaufman, N., E. J. Mason and T. D. Kinney: The effect of steroids on fibroblast migration in vitro. I. Cortisone its inhibitory effect. H. 17-Hydroxycorticosterone, its inhibitory effect. Amer. J. Path. 29, 761 (1953)
Kazakova, O. V., N. N. Orekhovich and V. O. Shpitiker: Effect of temperature on the rats of cleavage of procollagens by collagenase. Dokl. Akad. Nauk SSSR. 120, 359 (1958).
Keech, M. K.: The effect of collagenase on human skin collagen. Comparison of different age-groups and of cases with and without “Collagen Disease”. Yale J. Biol. Med. 26, 295 (1954).
Human skin collagen from different agegroups before and after collagenase digestion. An electron microscope study. Ann. rheum. Dis. 14, 19 (1955).
Transformation of collagen to elastin in dermal collagens with varying sensitivity towards collagenase. Ann. rheum. Dis. 17, 23 (1958).
Electron-microscope study of elastase-digested rat aorta. Gerontologia 4, 1 (1960).
Keech, M. K., and R. Reed: Electron-microscopic study of the effect of prolonged heat and ultraviolet light on human dermis from different age groups. Ann. rheum. Dis. 16, 198 (1957).
Kellgren, J. H., J. Ball, W. T. Astbury, R. Reed and E. Beighton: Biophysical studies of rheumatoid connective tissue. Nature (Lond.) 168. 493 (1951).
Kendrew, J. C., and M. F. Perutz: X-ray studies of compounds of biological interest. Ann. Rev. Biochem. 26, 327 (1957).
Kern,H. L.: Masked condition of ionic residues in collagen. Biochim. biophys. Acta 42, 345 (1960).
Kessler, A., H. Rosen and S. M. Levenson: Chromatographic fractionation of rat tail tendon collagen. Nature (Lond.) 184, Suppl. 21, 1640 (1959).
Chromatographic fractionation of acetic acid solubulized rat tail tendon collagen. J. biol. Chem. 235, 989 (1960).
Klauber, J. V., and H. Brown: Certain phases of sulfur metabolism of the skin. Arch. Derm. Syph. (Chicago) 34, 568 (1936).
Klenk, E., u. H. Faillard: Vorkommen von Neuraminsäure im Leberprotein bei amyloider Degeneration. Hoppe-Seylers Z. physiol. Chem. 299, 191 (1955).
Knobloch jr., W. H., P. Nagle, C. L. Shetlar and M. R. Shetlar: Effect of epidermal damage upon serum polysaccharides. Proc. Soc. exp. Biol. (N.Y.) 81, 417 (1952).
Kokas, E., I. Foldes and I. Banga: Elastase and trypsin contents of the pancreatic secretion. Acta physiol. Acad. Sci. hung. 2, 333 (1951). - Kodicek, E., and G. Loewi: The uptake of (35S) sulphate by mucopoly-saccharides of granulation tissue. Proc. roy. Soc. B 144, 100 (1955).
Konno, K., and K. I. Altman: Isolation of a glycine-carbohydrate residue from muscle collagen. Nature (Lond.) 181, 994 (1958).
Korn, E. D.: Synthesis of heparin by slices of mouse mast cell tumor. J. biol. Chem. 234, 1321 (1959a).
The isolation of heparin from mouse mast cell tumor. 234, 1325 (1959 b).
Enzymic sulfation of heparin. 234, 1647 (1959c).
Kowalsky, A., and D. E. Koshlandjr.: Mechanism of the galactose-glucose interconversion in Lactobacillusbulgaricus. Biochim. biophys. Acta 22, 575 (1956).
Kramer, H., and G. M. Windrun1: Sulfation techniques in histochemistry with special reference to metachromasia. J. Histochem. Cyto-chem. 2, 196 (1954).
Krompecher, ST., and GY. Berencsi: Mucopolysaccharides in the histochemistry of cancer. Production of neutral mucopolysaccharides and their drainage through dilated lymphatics in mouse cancer C3H. Acta morph. Acad. Sci. hung. 9, 375 (1958).
Kroner, T. D., W. Tabroff and J. J. Mcgarr: Peptides isolated from a partial hydrolyzate of steer-hide collagen. J. Amer. them. Soc. 75, 4084 (1953).
Evidence for the prolyl-hydroxyproline linkage in collagen. J. Amer. them. Soc. 77, 3356 (1955).
Kuhn, K., W. Grassmann and U. Hofmann: The electron microscopic definition of collagen and the production of highly subdivided cross striations. Z. Naturforsch. 13b, 154 (1958).
The formation of the collagen fibrils out of dissolved collagen and the function of the carbohydrate-containing components. Z. Naturforsch. 14b, 436 (1959).
Küun, K., U. Hofmann and W. Grassmann Querstreifung und Periodat-Silber-Urotropin-Reaktion bei verschiedenen Kollagenarten. Z. Naturforsch. 11 b, 581 (1956).
Die Verteilung basischer Aminosäuren im Tropokollagenmolekül. Naturwissenschaften 46, 512 (1959).
Kübnke, E.: The intrafibrillar network structure of collagen. Naturwissenschaften 44, 509 (1957).
Kulonen, E.: The free amino groups of citrate extracted collagen. Ann. Med. exp. Fenn. 33, 8 (1955).
Labella, F. S.: Elastin, a metabolically active lipoprotein. Nature (Lond.) 180, 1360 (1957).
Lamy, F., C. P. Craig and S. Tauber: Studies on elastase and elastin I. Assay and properties of elastase. J. biol. Chem. 236, 86 (1961).
Langecker, H.: Bestimmung der Hyaluronsäure in Organen. Klin. Wschr. 30, 222 (1952).
Larsen, B.: Presence of glycoproteins in secondary amyloid deposits related to serum glycoprotein. Acta rheum. stand. 3, 30 (1957).
Relation between the affinity for Congo red and the glycoprotein content of serum in rheumatoid arthritis and related diseases. Ann. rheum. Dis. 17, 240 (1958 a).
Metachromasia-inhibiting components in amyloid. J. Histochem. Cytochem. 6, 131 (1958b).
Laurent, T. C.: Comparative study of physicochemical properties of hyaluronic acid prepared according to different methods and from different tissues. Ark. Kemi 11, 487 (1957).
Layton, L. L.: In vitro sulfate fixation by granulation tissue and injured muscle tissue from healing wounds. Proc. Soc. exp. Biol. (N.Y.) 73, 570 (1950a).
Quantitative differential fixation of sulfate by tissues maintained in vitro. I. Sulfate fixation as a function of age. Cancer (Philad.) 3, 725 (1950b).
Effect of cortisone upon the tissue synthesis of acid mucopolysaccharides. Proc. Soc. exp. Biol. (N.Y.) 76, 596 (1951 a).
Bull. Schweiz. Akad med. Wiss. 8, 74 (1952).
Cortisone inhibition of mucopolysaccharides synthesis in the intact rat. Arch. Biochem. 32, 224 (1951b).
Layton, L. L., C. W. Denko, S. Scapa and D. R. Frankel: Influence of age upon chondroitinsulfate synthesis by the tissues of normal dba-mice. Cancer (Philad.) 5, 405 (1952).
Leloir, L. F.: The uridine coenzymes. 3. Internat. Congr. Brussels. Conf. and Reports 1955.
Leloir, L. F., and C. E. Cardini: Biosynthesis of glucosamine. Biochem. biophys. Acta 12, 15 (1953).
Biosynthesis of glycogen from uridine diphosphate glucose. J. Amer. them. Soc. 79, 6340 (1957).
Leloir, L. F., C. E. Cardini and J. M. Olavarria• Phosphorylation of acetylhexosamines. Arch. Biochem. 74, 84 (1958).
Leloir, L. F., M. A. Fekete and C. E. Cardini: Starch and oligosaccharide synthesis from uridine diphosphate glucose. J. biol. Chem. 236, 636 (1961).
Leloir, L. F., J. M. Olavarria, S. H. Goldemberg and H. Carminatti: Biosynthesis of glycogen from uridine diphosphate glucose. Arch. Biochem. 81, 508 (1959).
Lengyel, A., u. I. Szemesi: Hyaluronsäure-Untersuchung im Stroma des Plattenepithelkrebses am Gebärmutterhals. Gynaecologia (Basel) 140, 116 (1955).
Letterer, E., u. G. Schneider: Die Bedeutung des BluteiweiBbildes in der Amyloidose. Plasma (Milano) 1, 263 (1953).
Lewis, M. S., and K. A. Piez: Physical properties of dogfish shark skin collagen. Fed. Proc. 20, 380 (1961).
Lewis, U. J., D. E. Williams and N. G. Brink: Pancreatic elastase; purification, properties and function. J. biol. Chem. 222, 705 (1956).
Lillie, R D Studies on the preservation and histologic demonstration of glycogen. J. techn. Meth. 27, 23 (1947).
Lindner, I. J., H. A. Schweinitz and G. Freytag: Reactions of collagen fibers. Acta histochem. (Jena) 9, 231 (1960).
Lindstedt, S., and J. D. Prockop: Isotopic studies on urinary hydroxyproline as evidence for rapidly catabolized forms of collagen in young rat. J. biol. Chem. 236, 1399 (1961).
Linker, A., P. Hoffman and K. Meyer: The hyaluronidase of the leech: an endoglucuronidase. Nature (Lond.) 180, 810 (1957).
Linker, A., P. Hoffman, K. Meyer, P Sampson and E. D. Korn: The formation of unsaturated disaccharides from mucopolysaccharides and their cleavage to a keto acid by bacterial enzymes. J. biol. Chem. 235, 3061 (1960).
Linker, A., P. Hoffman, P. Sampson and K. Meyer: Heparitin sulfate. Biochim. biophys. Acta 29, 443 (1958).
Linker, A., K. Meyer and P. Hoffman: The production of unsaturated uronides by bacterial hyaluronidase. J. biol. Chem. 219, 13 (1956).
Lipmann, F.: Biological sulfate activitation and transfer. Science 128, 575 (1958).
Lipschitz, W. L., and E. Bueding: Mechanism of the biological formation of conjugated glucuronic acids. J. biol. Chem. 129, 333 (1939).
Lison, L.: Etudes sur la metachromasie. Colorants metachromatiques et substances chromotropes. Arch. Biol. (Liège) 46, 599 (1935).
Histochimie et cytochimie animales. Paris: Gauthier-Villars 1953.
Alcian blue 8 G with chlorantine-fast red 5 B. A technique for selective staining of muco-polysaccharides. Stain Technol. 29, 131 (1954).
Loewi, G.: Urinary excretion of acid polysaccharide in rheumatoid arthritis and other diseases. Ann rheum. Dis. 18, 239 (1959).
Loewi, G., L. E. Glynn and J. Dorling: The nature of collagen degeneration. J. Path. Bact. 80, 1 (1960).
Loewi, G., and P. W. Kent: The utilization of inorganic sulfate by granulation tissue. Biochem. J. 65, 550 (1957).
Loewi, G., and K. Meyer: Acid muco-polysaccharides of embryonic skin. Biochim. biophys. Acta 27, 453 (1958).
Loomeijer, F. J.: Yellow fluorescent pigment in elastin. Nature (Lond.) 182, 182 (1958).
Lorenzoni,L.: Comportamento delle mucoproteine del sottocute di ratti normali e portatori di sarcoma Galliera tratti con dietilstilbene. Atti Soc. lombarda Sci. med. biol. 10, 201 (1955).
Comportamente delle mucoproteine percloricosolubili plasmatiche e del tessuto connettivo sottocutaneo di ratti portatori di alcuni tumori da innesto. Tumori 42, 361 (1956a).
Variazioni dei contenuto in mucoproteine percloricosolubili del plasma e del connetivo in ratti trattiati con estrogeni di sintesi. Tumori 42, 431 (1956b).
Lowry, O. H., D . Gilligan and E. M. Katersky: The determination of collagen and elastin in tissues, with results obtained in various normal tissues from different species. J. biol. Chem. 139 , 795 (1941).
Lowther, D. A., and H. J. Rogers: The role of glutamine in the biosynthesis of hyaluronate by streptococcal suspensions. Biochem. J. 62, 304 (1956).
Ludwig, A. W., and N. F. Boas: The effects of testosterone on the connective tissue of the comb of the cockerel. Endocrinology 46. 291 (1950).
Ludwig, A. W., N. F. Boas and L. J. Soffer: Rôle of mucopolysaccharides in pathogenesis of experimental exophthalmos. Proc. Soc. exp. Biol. (N.Y.) 73, 137 (1950).
Lustig, B., and E. Nassau: The carbohydrate content of the proteins in blood serum, cantharidin blisters and pleural effusions. Amer. Rev. Tuberc. 6, 817 (1941).
Lynnjr., W. S.. R. Brown and E. Earnhardt: Effects of starvation on metabolism and enzyme contents of adipose tissue. Fed. Proc. 20, 204 (1961).
MA, C. K.: Morphological and chemical investigation of dermal elastic and collagenic tissue during epidermal carcinogenesis. Cancer Res. 9, 481 (1949).
MA, C. K., and E. V. Cowdry: Aging of elastic tissue in human skin. J. Geront. 5, 203 (1950).
Malaprade, L.: Action des polyalcools sur l’acide periodique. Application analytique. Bull. Soc. chim. Fr., Ser. IV 43, 683 (1928).
Etude de l’action des polyalcools sur l’acide periodique et les periodates alcalins. Bull. Soc. chim. Fr., Ser. V 1, 833 (1934).
Malawista, I., and M. Schubert: Chondromucoprotein new extraction method and alkaline degradation. J. biol. Chem. 230, 535 (1958).
Mancini, R. E.: Inhibition of fibroplasia of keloids by the local action of hydrocortisone. Rev. Soc. argent. Biol. 30, 107 (1954).
Mancini, R. E., y I. Bacarini: Mucoproteinas du tejido conectivo adulto y embrionario. Rev. Soc. argent. Biol. 27, 27 (1951).
Mancini, R. E., I. Izquierdo and P. Kirschbaum: Influence of testosterone on fixation of sulfur-35 by the mucopolysaccharides of connective tissue of the cock’s comb. C. R. Soc. Biol. (Paris) 152, 190 (1958).
Mandl, I . , and S. F. Zaffuto. Serological evidence for a specific Clostridium histolyticum gelatinase. J. gen. Microbiol. 18, 13 (1958).
Mandl, I., H. Zipper and L. T. Ferguson: Clostridium histolyticum collagenase: its purification and properties. Arch. Biochem. 74, 465 (1958).
Marriott, R. H.: The swelling of single collagen fiber bundles. Biochem. J. 26, 46 (1932).
Masamune, H.: On the mode of combination of carbohydrate with amino acid grouping in mucopolysaccharides and mucoproteins. Conferences et Rapports 3 eme Congres. Internat. de Biochimie, Bruxelles, 1955.
Masamune, H . , M. Suzuki and Y. Kondoh: Heparin. J. Biochem. (Tokyo) 31 , 343 (1940).
Mathews, M. B.: The molecular weight of sodium chondroitinsulfate by light scattering. Arch. Biochem. 61, 367 (1956).
Isomeric chondroitinsulphates. Nature (Lond.) 181, 421 (1958).
Acid strength of carboxyl groups in isomeric chondroitinsulfates. Biochim. biophys. Acta 48, 402 (1961).
Mathews, M. B., and I. Lozaityte: Sodium chondroitinsulfate-proteins complexes of cartilage. I. M.lecular weight and shape. Arch. Biochem. 74, 158 (1958).
Matthews, V. J., J. K. Newton and W. R. Bloor: The lipides of the skin in experimental diabetes. J. biol. Chem. 108, 145 (1935).
Mayer, R. L.: Hyaluronidase and inflammation of the skin. Ann. N.Y. Acad. Sci. 52, 1041 (1950).
Mazurov, V. I., and V. N. Orekhovich: a-and -components of procollagens. Biokhimiya 25, 814 (1960).
Mcclean, D.: The influence of testicular extract on dermal permeability and the response to vaccine virus. J. Path. Bact. 33, 1045 (1930).
Mccready, R. M., H. A. Swenson and W. D. Maclay: Determination of uronic acids. Industr. engng. Chem. II 18, 290 (1946).
Mcgavack, T. H., and K. Y. T. KAO: Influence of age and sex on the soluble collagen, insoluble collagen, and elastin of rat tissues. Exp. Med. Surg. 18, 104 (1960).
Mcmaxus, F. J. A.: Histological demonstration of mucin after periodic acid oxidation. Nature (Loud.) 158, 202 (1946).
Histological and histochemical uses of periodic acid. Stain Technol. 33, 99 (1948).
Carbohydrate specificity of the periodic acid-Schiff’s reagent. Amer. J. Path. 26, 690 (1950).
Mcmanus, J. F. A.. and J. C. Cason: Carbohydrate histochemistry studied by acetylation techniques. I . Periodic acid methods. J. exp. Med. 91, 651 (1950) .
Mechanic, G., and M. Levy: An r-lysine tripeptide obtained from collagen. J. Amer. chem. Soc. 81, 1889 (1959).
Mende, T. J.. and E. L. Chambers: Reaction of tissues with Schiff’s reagent after treatment with anhydrous ehromylchloride. J. Histochem. Cytochem. 5, 606 (1957).
Merchant, D . J., and R. H. Kahn: Fiber formation in suspension cultures of L strain fibroblasts. Proc. Soc. exp. Biol. (N.Y.) 97 , 359 (1958).
Meyer, K.: Chemical structure of hyaluronic acid. Fed. Proc. 17, 1075 (1958).
Studies on Hurler’s syndrome. Canad. med. Ass. J. 84, 851 (1961).
Meyer, K., and E. Chaffee: The mucopolysaccharides of skin. J. biol. Chem. 138, 491 (1941).
Meyer, K., M. M. Grumbach, A. Linker and P. Hoffman: Excretion of sulfated muco-polysaccharides in gargoylism. Proc. Soc. exp. Biol. (N.Y.) 97, 257 (1958).
Meyer, K., G. L. Hobby, E. Chaffee and M. H. Dawson: Hydrolysis of hyaluronic acid by bacterial enzymes. J. exp. Med. 71, 137 (1940).
Meyer, K., and J. W. Palmer: On glycoproteins. II. The polysaccharides of vitreous humor and of umbilical cord. J. biol. Chem. 114, 689 (1936).
Meyer, K., E. M. Smyth and M. H. Dawson: The isolation of a mucopolysaccharide from Synovial fluid. J. biol. Chem. 128, 319 (1939).
Michaelis, L.: Reversible polymerization and molecular aggregation. J. physic. Colloid Chem. 54, 1 (1950).
Michaels, S., P. M. Gallop, S. Seifter and E. Meilman: Specificity of collagenase. Biochim. biophys. Acta 29, 450 (1958).
Mikolajczyx, H.: The effect of follicle-stimulating hormone and castration on mucopolysaccharides of connective tissue. Endokrynol. Polska 10, 91 (1959).
Mirski, A.: Metabolism of adipose tissue in vitro. Biochem. J. 36, 232 (1942).
Mirsky, A. E., and H. Ris: Variable and constant components of chromosomes. Nature (Lond.) 163, 666 (1949).
Mitoma, C., and T. E. Smith: Studies on the role of ascorbutic acid in collagen synthesis. J. biol. Chem. 235, 246 (1960).
Mombelloni, P., C. L. Pirani and H. R. Catch-Pole: Serum proteins and glycoproteins in experimental scurvy and in carrageenan granuloma. Fed. Proc. 20, 160 (1961).
Montagna, W., and C. R. HILL The localization of sulfur-35 in the skin of the rat. Anat. Rec. 127, 163 (1957).
Moret, V., and L. Gotte: The mechanism of action of elastase. Atti R. Accad. naz. Lincei, Cl. Sci. fis., mat. natur. 23, 442 (1957).
Morris, C. C., and G. C. Godman: Production of acid mucopolysaccharides by fibroblasts in cell cultures. Nature (Lond.) 188, 407 (1960).
Moss, J. A.: The carbohydrate of collagen. Biochem. J. 61, 151 (1955).
Movat, H. Z., R. H. More and D. Wolocaow: Cellular and intercellular changes after mechanical chemical or radiation injury of connective tissue. Brit. J. exp. Path. 41, 97 (1960).
Müller, G.: A simplification of the Hale reaction. Acta histochem. (Jena) 2, 68 (1955).
Demonstration of acid mucopolysaccharides by toluidine blue metachromasia, alcian blue, the periodic acid-Schiff reaction, and the ferric hydroxid periodic acid-Schiff reaction. Acta histochem. (Jena) 6, 218 (1959).
Munchpetersen, H., M. Kalckar, E. Cutolo and E. B. Smith: Uridyl transferases and the formation of uridine triphosphate. Enzymic production of uridine triphosphate: uridine diphosphoglucose pyrophosphorolysis. Nature (Lond.) 172, 1035 (1953).
Municio, A. M., and M. Mallol• Some aspects of the metabolism of D-glucosamine. Bull. Soc. Chim. biol. (Paris) 39, Suppl., 194 (1957).
Nagai, Y., S. Sakakibara, H. Noda and S. Akabori: Hydrolysis of synthetic peptides by collagenase. Biochim. biophys. Acta 37, 567 (1960).
Nageotte, J.: Fibrillous coagulation in vitro of collagen dissolved in a dilute acid. C. R. Acad. Sci. (Paris) 184, 115 (1927).
Surla solubilité du collagène dans les acides dilués. C. Rend. Soc. Biol. (Paris) 98, 15 (1928).
Nakajima, T., E. Kimoto and M. Karizoe: Histochemical demonstration of chondroitinsulfuric acid and related substances. Ugaku to Seibutsugaku 36, 182 (1955).
Naughton, M. A., and F. Sanger: Purification and specificity of pancreatic elastase. Biochem. J. 78, 156 (1961).
Nemeth-Csoka, M.: Studies on collagen fibers. I. The submicroscopic structure on in vitro precipitated collagen fibers and the stabilizing rôle of acid mucopolysaccharides. Acta histochem. (Jena) 9, 282 (1960).
Nemetschek, TH.: Morphology of collagen: transverse structure, elementary fibrils, and arrangement in cell bands. Naturforsch. 13 b, 225 (1958).
Neuberger, A.: Observations on the presence and metabolism of plasma proteins in skin and tendon. In Symposium Council for International Organizations of Medical Sciences, p. 35, London 1956.
Metabolism of collagen in mammals Arzneimittel-Forsch. 10 , 390 (1960).
Neuberger, A., and H. G. Slack: The metabolism of collagen from liver, bone, skin and tendon in the normal rat. Biochem. J. 53, 47 (1953).
Neuman, R. E.: The amino acid composition of gelatins, collagens, and elastins from different sources. Arch. Biochem. 24, 289 (1949).
Neuman, R. E., and M. A. LOGAN: The determination of hydroxyproline. J. biol. Chem. 184, 299 (1950a).
The determinations of collagen and elastin in tissues. J. biol. Chem. 186, 549 (1950b).
Neville-Jones, D., and R. Peters: A further observations on the proteolytic enzymes in rat skin. Biochem. J. 43, 303 (1948).
Nicolet, B. H., and L. A. Sewn The action of periodic acid on amino alcoholic. J. Amer. chem. Soc. 61, 1615 (1939).
Niseigai, M., Y. Nagai and H. Noda: Partial collagenase digestion of the fiber structure of collagen. J. Biochem. (Tokyo) 48, 152 (1960).
Nishieara, T., and P. Doty: Sonic fragmentation of collagen macromolecules. Proc. nat. Acad. Sci. (Wash.) 44, 411 (1958).
Noda, H.: Physico-chemical studies on the soluble collagen of rat tail tendon. Biochim. biophys. Acta 17, 92 (1955).
Odeblad, E., and D Zmiorro: Uptake of radio sulfate in different organs after total body irradiation. Acta radiol. (Stockh.) 44, 313 (1955).
Ogston, A. G., and J. E. Stanier: A micromethod for the estimation of uronic Acid. Biochem. J. 49, 591 (1951).
Oxen, D. E., and R. J. Bouler: Enzymic proteolysis of rat sponge-biopsy collagen tissue. Proc. Soc. exp. Biol. (N.Y.) 96, 367 (1957).
Oneson, I., and J. Zacharis: The role of the carbohydrate moiety in the structure of the collagen fibril. Arch. Biochem. 89, 271 (1960).
Opsajl, J. C.: The role of certain steroids in the adrenal-hyaluronidase relationship. Yale J. Biol. Med. 22, 115 (1949).
Orekhovich, K. D.: Procollagen content of the skin of animals at various age levels. Dokl. Akad. Nauk SSSR. 71, 521 (1950).
Orekhovich, V. N.: Specific alterations of skin proteins. Byull. Eksptl. Biol. Med. 22, 57 (1946).
Orekhovich, V. N., A. S. Konikova, K. 1). Orekhovich and V. N. Dobbert: The rate of renewal of proteins of various tissues and organs. Dokl. Akad. Nauk SSSR. 71, 105 (1950).
Orekhovich, V. N., and L. V. Pavlikhina: Transformation of procollagen into collagen. Vopr. med. Khim. 3, 195 (1957).
Orekhovich, V. N., L. V. Pavlikhina and V. O. Shpikiter: The nature of the alkalisoluble collagen fraction. Biokhimiya 22, 210 (1957).
Orekhovich, V. N., and V. O. Shpikiter: Study of some properties of denaturated procollagen with the ultracentrifuge. Dokl. Akad. Nauk SSSR. 101, 529 (1955a).
Molecular weight and the degree of asymmetry of procollagen. Biokhimiya 20, 438 (1955 b).
Procollagens as biological precursors of collagen and the physico-chemical nature of these proteins. Connective Tissue, Symposium. Council for Internat. Organizations of Medical Science, p. 281, London 1956.
Isolation of a and ß components of procollagen. Dokl. Akad. Nauk SSSR. 115, 137 (1957).
Procollagens. Science 127, 1371 (1958).
Orekhovich, V. N., V. O. Shpikiter, O. Kasakova and V. Mazurov: The incorporation of C14-labeled glycine into the a-and B components of procollagen. Arch. Biochem. 85, 554 (1959).
Orekhovich, V. N., V. O. Shpikiter and V. T. Zaslavskii: Sedimentation and diffusion of a-B components of procollagen and their ratio. Biokhimiya 23, 285 (1958).
Orekhovich, V. N., A. A. Tustanovsxii and K. D. Orekhovich: Enzymic hydrolysis of crystalline skin protein. Dokl. Akad. Nauk SSSR. 57, 475 (1947).
Orekhovich, V. N., A. A. Ttjstanovskii, K. D. Orekhovich and N. E. Plotnikova: The procollagen of hide. Biokhimiya 13, 55 (1948).
Orekhovich, V. N., A. A. Tustanovskli and N. E. Plotnikova: Isolation of crystalline proteins of a new type (procollagen) from various organs of the vertebrates. Dokl. Akad. Nauk SSSR. 60, 837 (1948).
Riexhovitch, V. N.: Les procollagènes, composition chimique. Propriétés et rôle biologique. IIe Congr. Internat. de biochimie Paris, Symposium sur la biogénèse des protéines, p. 62, 1952. — ORLOVSKAYA
V., A. L. Zaides and A. A. Tustanovsxm: Formation of collagen in embryogenesis. Dokl. Akad. Nauk Sssr. 111, 1396 (1956).
Orr, S. F. D.: Infra-red spectroscopic studies of some polysaccharides. Biochim. biophys. Acta 14, 173 (1954).
Ozzello, L., E. Y. Lasfargues and M. R. Murray: Growth-promoting activity of acid mucopolysaccharides on a strain of human mammary carcinoma cells. Cancer Res. 20, 600 (1960).
Partridge, S. M.: Chemistry of connective tissues. I. The fate of combination of Chondroitinsulfate In Cartilage. Biochem. J. 43, 387 (1948).
Partridge, S. M., and H. F. Davis: The chemistry of connective tissues. 3. Composition of the soluble proteins derived from elastin. Biochem. J. 61, 21 (1955).
The presence in cartilage of a complex containing chondroitinsulfate combined with noncollagenous protein. Ciba Found. Symp. Chem. Biol. Mucopolysaccharides, p. 93, 1958.
Partridge, S. M., H. F. Davis and G. D. Adair: The chemistry of connective tissues. 2. Soluble proteins derived from partial hydrolysis of elastin. Biochem. J. 61, 11 (1955).
Paschoud, J. M.: Experimentelle Untersuchungen zur Heparin-Genese der Urticaria pigmentosa. Dermatologica (Basel) 108, 362 (1954).
Pauling, L., and R. B. Corey: Structure of fibrous proteins of the collagen gelatin group. Proc. nat. Acad. Sei. (Wash.) 37, 272 (1951).
Pearce, R. H., and E. M. Watson: Mucopolysaccharides of human skin. Canad. J. Res. E 27, 43 (1949).
Penney, J. R., and B. M. Balfour: The effect of vitamin C in mucopolysaccharide production in wound healing. J. Path. Bact. 61, 171 (1949).
Pernis, P., and E. Clerici: Chemobiological studies of hyaline tissue in silicosis. Carbohydrate content. Med. d. Lavoro 48, 238 (1957).
Persson, B. H.: Studies on connective tissue ground substance. I. Histochemical features of ground substance in ascorbic acid deficiency and its modification by the action of cortisone. Acta Soc. Med. upsalien. 58, 120 (1953).
Peters, R. A., and R. W. Wakelin: The effect of some thiol compounds upon trypsin, chymotrypsin and chymotrypsinogen. Biochem. J. 43, 45 (1948).
Pfeiffer, H. H.: The topochemical analysis of glycoproteins in amyloid deposits. Acta histochem. (Jena) 8, 97 (1959).
Pierce, J. W . A., R. H. Steele and A. G. C. White: A colorimetric method for hyaluronic acid estimation. Proc. Soc. exp. Biol. (N.Y.) 83, 373 (1953).
Piez, K. A., and J. Gross: The amino acid composition of some fish collagens. The relation between composition and structure. J. biol. Chem. 235, 995 (1960).
Piez, K. A., and R. C. Likins: The conversion of lysine to hydroxylysine and its relation to the biosynthesis of collagen in several tissues of the rat. J. biol. Chem. 229, 101 (1957).
Piez, K. A., E. Weiss and M. S. Lewis: Separation and characterization of the a and ß components of calf-skin collagen. J. biol. Chem. 235, 1987 (1960).
Pikulev, A. T.: Elastin as a glycolipoprotein. Shorn. Nauch Rabot Stalingrad Med. Inst. 11, 45 (1957).
Pirani, C. L., andH. R. Catchpole: Serum glycoproteins in experimental scurvy. A.M.A. Arch. Path. 51, 597 (1951).
Plotnikova, N. E.: Isolation of crystalline proeollagens from skin and organs of man. Dokl. Akad. Nauk SSSR. 66, 1145 (1949).
Pontis, H. G.: Uridine diphosphate acetylgalactosamine in liver. J. biol. Chem. 216, 195 (1955).
Pouradier, J., and M. Abri-Bat: Analysis of various hypotheses on the structure and constitution of gelatin. Science inds. phot. 20, 444 (1949).
Pouradier, J., and A. M. Venet: The structure of gelatin. II. Variation of the physical and mechanical properties with molecular weight. J. Chim. Physique 47, 391 (1950).
Prodi, G., e F. Cantelli: Sul contenuto di esoamine in organi di animale sottoposti ad amiloidose spermentale. G. Biochim. 4, 58 (1955).
Pugh, D., D. H. Leobacx and P. G. Walker: Studies on glucosaminidase N-Acetyl glucosaminidase in rat kidney. Biochem. J. 65, 464 (1957).
Radino, G.: Histophotometric research on the behavior of the interstitial mucoid substance under the action of ultrasounds. Med. sper. 28, 302 (1956).
Ragan, C., E. L. Howes, C. M. Plotz, K. Meyer and J. W. Blunt: Effect of cortisone on the production of granulation tissue in the rabbit. Proc. Soc. exp. Biol. (N.Y.) 72, 718 (1949).
Ramachandran, G. N.: Infrared spectrum and structure of collagen. J. Chem. Physics 23, 600 (1955).
Structure of collagen. Nature (Lond.) 177, 710 (1956).
Ramachandran G. N., and G. Kartha: Structure of collagen. Nature (Lond.) 174, 269 (1954).
Ramackandran, G. N., and M. S. Santhanam: Structure of elastin. Proc. ind. Acad. Sei. A 45, 124 (1957).
Rapport, M. M., B. Weissmann, A. Linker and K. Meyer: Isolation of a crystalline disaccharide, hyalobiuronic acid, from hyaluronic acid. Nature (Lond.) 168, 996 (1951).
Rask-Nielson, R., J. Clausen and H E Christensen: II. Paper electrophoretic investigations on serum and urine of mice with experimental amyloidosis. Protides. Biol. Fluids. Proc. 7th, Colloq. Bruges, Belg., p. 190, 1960.
Reissio, J. L.: Phosphoacetylglucosaminemutase of Neurospora. Act. bioquim. (Rosario, Arg.) 2, 52 (1953).
J. biol. Chem. 219, 753 (1956).
Rich, A., and F. H. C. Crick: Structure of collagen. Nature (Lond.) 176, 915 (1955).
Rieder, S. V., and J. M. Buchanan: Studies on the biological formation of glucosamine in vivo. J. biol. Chem. 232, 959 (1958).
Rienits, K. G.: Acid mucopolysaccharides of the sexual skin of apes and monkeys. Biochem. J. 74, 27 (1960).
Riley, J. F.: The effects of histamine liberators on the mast cells of the rat. J. Path. Bact. 65, 471 (1953).
Mast cells. Livingstone: E. 0026 S. 1959.
Riley, J. F., and G. B. West: The presence of histamine in tissue mast cells. J. Physiol. (Loud.) 120, 528 (1953).
Rinehart, J. F., and K. Abdul-Haj: An improved method for the histologic staining of acid polysaccharides and 1,2-glycol groupings in paraffin sections of rat tissue. Amer. J. Path. 26, 639 (1950).
Rizzoli, C.: The histochemical basis for the staining of mucopolysaccharides in tissues with Alcian blue 8 GN. Boll. Soc. ital. Biol. sper. 31, 420 (1955).
Robbins, P. W., and F. Lipmann: Identification of enzymically active sulfate as adenosine-3-phosphate-5-phosphosulfate. J. Amer. them. Soc. 78, 2652 (1956).
Isolation and identification of active sulfate. J. biol. Chem. 229, 837 (1957).
Enzymatic synthesis of adenosine-5’-phosphosulfate. J. biol. Chem. 233, 686 (1958).
Robb-Smith, A. H. T.: The relation of reticulin to other collagens. Proc. Conf. Gelatine and Glue Research, p. 38, 1957.
Robert, L . , and P. Samuel: Spectrophotometric method for determination of the elastase inhibitor of serum. Ann. Biol. clin. 15 , 453 (1957).
Robertson, W. V. B., and H. Hinds: Polysaccharide formation in repair tissue during ascorbic acid deficiency. J. biol. Chem. 221, 791 (1956).
Robertson, W. V. B., J. Hiwett and C. Herman: The relation of ascorbic acid to the conversion of proline to hydroxyproline in the synthesis of collagen in the carageenan granuloma. J. biol. Chem. 234, 105 (1959).
Robertson, W. V. B., M. W. Ropes and W. Bauer: Mucinase; a bacterial enzyme which hydrolyzes synovial fluid mucin and other mutins. J. biol. Chem. 133, 261 (1940).
Robertson, W. V. B., and B. Schwartz: Ascorbic acid and the formation of collagen. J. biol. Chem. 201, 689 (1953).
Rodén, L.: Effect of hexosamines on the synthesis of chondroitin sulphuric acid in vitro. Ark Kemi 10, 345 (1956).
Roden, L., and A. Dorfman: The metabolism of mucopolysaccharides in mammalian tissues. The origin of 1-iduronic acid. J. biol. Chem. 233, 1030 (1958).
Rodesch, J., and P. Mandel: Ribonucleic acid in the skin of the white rat. Bull. Soc. franç. Derm. Syph. 64, 561 (1957).
Romani, J. D.: Comparative inhibiting action of cortisone and 17-hydroxycorticosterone on the inflammatory granuloma and on local and general eosinophilia during formation of a fixation abscess in the rat. C. R. Soc. Biol. (Paris) 147, 970 (1953).
Action of anti-inflammatory corticoids on the fibroblasts and mucopolysaccharides of a fixation abscess in the rat. C. R. Soc. Biol. (Paris) 148, 37 (1954).
Romanini, M. G., e A. R. Giordano: Contributi allo studio dei mucopolisaccaridi. II. Osservazioni sullo studio della metacromasia e di altre reazioni di sostanze mucoidi dopo ossidazioni varie. Mikroskopie 7, 26 (1952).
Ropes, M. W., W. V. B. Robertson, E. Rossmeisl, R. B. Peabody and W. Bauer: Synovial fluid mucin. Acta med. stand. Suppl. 196, 700 (1947).
Roseman, S., F. E. Moses, J. Ludowieg and A. Dorfman: The biosynthesis of hyaluronic acid by group A streptococcus. Utilization of glucose-1 -carbon“. J. biol. Chem. 203, 213 (1953).
Rosen, H., A. Kessler and S. M. Levenson: Metabolic inhomogeneity of rat tail tendon collagen: The distribution of Cu in the chromatographic components. Arch. Biochem. 90, 167 (1960).
Ross, R., and E. P. Bennrrr: A comparison of the ultrastructure
sequences in normal versus scorbutic wounds. Fed. Proc. 20, 164 (1961).
Rowen, J. W., and R. Brunish: The size and shape of hyaluronic acid from vitreous humor. Atomic Energy Comm. UCLA-326, 39 pp., 1955.
Rowen, J. W., R. Brunish and F. W. Bishop: Form and dimensions of isolated hyaluronic acid. Biochim. biophys. Acta 19, 480 (1956).
Sakata, R.: Biochemical studies on collagen metabolism. I. Collagen metabolism in normal skin. Kumamoto med. J. 13, 27 (1960).
Salvini, L., and M. Concella: The elastase inhibitor in serum. Arch. Stud. Fisiopat. Ricambio 21, 460 (1957).
Sanger, F.: Free amino groups of insulin. Biochem. J. 39, 507 (1945).
Santos, P. S., H. S. Santos, G. A. Edwards, A. R. Hoge and P. Sawaya: Contribution to the knowledge of the fine structure and chemical properties of animal connective tissue fibers. Mem. Inst. Butantan 27, 1 (1955/56).
Sasisekharan, V., and G. N. Ramachandran: Collagen. Il. Cylindrical lattice structure of collagen. Proc. ind. Acad. Sci. A 45, 363 (1957).
Satake, M.: Itinsulfuric acid in pig skin. II. Two disaccharides isolated from skin itinsulfate. Tôhoku J. exp. Med. 68, 385 (1958).
Satake, M., and H. Masamune: Two disaccharides separated from a probable mixture of dermoitinsulfuric and chondroitinsulfuric acids. Tôhoku J. exp. Med. 68, 44 (1958).
Scarselli, V.: Spectrophotometric determination of elastin. G. Biochim. 7, 20 (1958).
Schiller, S.: The influence of the thyroid gland on metabolism of muco-polysaccharides in the skin of rats. Fed. Proc. 20, 163 (1961).
Schiller, S, E. O. Benditt and A. Dorfman: Effect of testosterone and cortisone on the hexosamine content and metachromasia of chick combs. Endocrinology 50, 504 (1952).
Schiller, S, and A. Dorfman: Biosynthesis of mucopolysaccharides in the skin of alloxan-diabetic rats. Biochim. biophys. Acta 16, 304 (1955).
The metabolism of mucopolysaccharides in animals: the influence of insulin. J. biol. Chem. 227, 625 (1957a).
The metabolism of mucopolysaccharides in animals; the effect of cortisone and hydrocortisone on rat skin. Endocrinology 60, 376 (1957b).
Schiller, 8., M. B. Mathews, J. A. Cifonelli and A. Dorfman: The metabolism of mucopolysaccharides in animals. Further studies on skin of glucose-C14, acetate-C“, and sodium sulfate-S33. J. biol. Chem. 218, 139 (1956).
Schiller, S., M. B. Mathews, L. Goldfaber, J. Ludowieg and A. Dorfman: The metabolism of mucopolysaccharides in animals. Studies in skin utilizing labelled acetate. J. biol. Chem. 212, 531 (1955).
Schiller, S., M. B. Mathews, H. Jefferson, J. Ludowieg and A. Dorfman: The metabolism of mucopolysaccharides in animals. Isolation from skin. J. biol. Chem. 211, 717 (1954).
Schiller, S., G. A. Slover and A. Dorfman: A method for the separation of acid muco-polysaccharides: Its application to the isolation of heparin from the skin of rats. J. biol. Chem. 236, 983 (1961).
Schilling, J. A., and L. E. MILcH: Fractional analysis of experimental wound fluid. Proc. Soc. exp. Biol. (N.Y.) 89, 189 (1955).
Schlack, P., and W. Kumpf: A new method for ascertaining the constitution of peptides. Hoppe-Seylers Z. physiol. Chem. 154, 125 (1926).
Sehmitt, F. O.: The macromolecular basis of collagen structure. Conf. on connective tissue, thrombosis and atherosclerosis, edit. by IRVINE H. Page, p. 43. (Academic Press 1959 ).
Sehmitt, F. O., and J. Gross: Further progress in the electron microscopy of collagen. J. Amer. Leather Chemists ’ Ass. 43, 658 (1948).
Schmitt, F. O., J. Gross and J. H. Highberger: A new particle type in certain connective tissue extracts. Proc. nat. Acad. Sci. (Wash.) 39, 459 (1953).
States of aggregation of collagen. Symposia Soc. Exp. Biol. No 9, Fibrous Proteins and their Biol. Significance 148 (1954).
Sehmitt, F. O., C. E. Hall and M. A. Jakus: Investigations of collagen by electron microscope. J. cell. comp. Physiol. 20, 11 (1942).
Sehmitt, F. O., and A. J. Hodge: Das Tropokollagen-Makromolekül und die Eigenschaften seiner geordneten Aggregations-formen. Leder 11, 74 (1960).
Scxöll, H., I. Bennhold and P. B. Diezel: Verschiedene Typen von Farbänderungen von Azofarbstoffen. Ein Beitrag zur Metachromasie. Histochemie 1, 315 (1959).
Schroeder, W. A., L. M. Kay, J. LE Cette, L. Honnen and F. C. Green: The constitution of gelatin. Separation and estimation of peptides in partial hydrolyzates. J. Amer. chem. Soc. 76, 3556 (1954).
Schrohenloher, R. E., J. D. Ogle and M. A. Logan: Two tripeptides from an enzymatic digest of collagen. J. biol. Chem. 234, 58 (1959).
Schubert, M., et A. Levine: A conductimetric study of the interaction of anionic mucopolysaccharides and cationic dyes. J. Amer. chem. Soc. 75, 5842 (1953).
Schwarz, W., and H. J. Merker: Electron-microscopic investigations of internal silvering of the tendon fibril. Histochemie 1, 225 (1959).
Seeberg, G.: Cutaneous absorption during the menstrual cycle and its influence on intradermal reactions of the delayed type. Acta derm.-venereol. (Stockh.) 30, 231 (1950).
Seifter, S., P. M. Gallop, L. Klein and E. Meilman: Il. Properties of purified collagenase and its inhibition. J. biol. Chem. 234, 285 (1959).
Setala, K., P. Holsti, S. Lundbom, L. Merenmies and K. Dammert: Die Wirkung nicht ionisierbarer, oberflächenaktiver, tumorerregender Substanzen auf das Kollagen der Kaninchenhaut. Z. Krebsforsch. 61, 569 (1957).
Shallock, G.: The process of glycoprotein dissociation in ground substance of connective tissue. Bull. Soc. franç. Derm. Syph. 64, 636 (1957).
Shapiro, B., and E. Wertheimer: The synthesis of fatty acids in adipose tissue in vitro. J. biol. Chem. 173, 725 (1948).
Shatton. J., and M. Sohu Bert: Isolation of a mucoprotein from cartilage. J. biol. Chem. 211, 565 (1954).
Sheehan, J. C., and W. A. Boiaofer: A new isolation of hydroxylysine. J. Amer. them. Soc. 72, 2466 (1950).
Sherry, S., W. Troll and E. D. Rosenblum: Collagenase activity of cathepsins. Proc. Soc. exp. Biol. (N.Y.) 87, 125 (1954).
Shetlah, M. R., E. G. Lacefield, B. N. White and J. A. Schilling: Wound healing: glycoproteins of wound tissue. I. Hexosamine, hexose and uronic acids content. Proc. Soc. exp. Biol. (N.Y.) 100, 501 (1959).
Shirai, Y., and T. Ohkubo: Synthesis of glucuronides by tissue slices. J. biol. Chem. 41, 341 (1954).
Sinex, F. M., and B. Faris• The pigmentation of elastin. Fed. Proc. 20, 378 (1961).
Sinex, F. M., and D. D. Van Slyre: The source and state of the hydroxylysine of collagen. J. biol. Chem. 216, 245 (1955).
Slack, H. G. B.: The metabolism of sulphated polysaccharides in carageenin induced granuloma. Biochem. J. 64, 7p. (1956).
Connective tissue growth stimulation by carageenin. II. The metabolism of sulfate polysaccharides. Biochem. J. 65, 459 (1957).
Connective tissue growth stimulated by carageenin. III. The nature and amount of polysaccharide produced in normal and ascorbutic guinea pigs and the metabolism of a chondroitinsulfuric acid fraction. Biochem. J. 69, 125 (1958).
Smith, E. E. B., and G. T. Mills Uridyl transferase of mammary gland. Biochim. biophys. Acta 18, 151 (1955).
Smith, H.: The virulenceenhancing factor of mucins. Fractionation studied on hog gastric mucins. Biochem. J. 46, 356 (1950).
Identification of a heparin as a main component of the “third factor” involved in the virulence-enhancing action of hog gastric mucin. Nature (Loud.) 168, 563 (1951).
Smith, H., P. W. Harris-Smith and J. L. Stanley: The virulence-enhancing factor of mucins. The role of particulate insoluble matter and a viscous medium in virulence enhancement, with a revised assay of the third factor involved. Biochem. J. 50, 211 (1951).
The virulence-enhancing factor of mucins. Identification of a heparin as the main component of the third factor involved in virulence enhancement. Biochem. J. 52, 22 (1952).
Smith, J. E., G. T. Crowley jr. and R. B. Giles jr Some carbohydrates of synovial fluid. Arthritis Rheumat. 3, 409 (1960).
Smith, R. H., and S. Fitton-Jackson: Conversion of L-proline-C14 to hydroxyproline-C14 by fowl osteoblasts in tissue culture. J. biophys. Biochem. Cytol. 3, 912 (1957).
Smits, G., J. Morreau, C. Garcia-Smit and S. Stodel: Quantitative interrelations of the chief components of some connective tissues during fetal and post-natal development in cattle. Biochim. biophys. Acta 25, 542 (1957).
Sobel, H., S. Gabay and G. Boxorrls: Hexosamine and collagen in tissue of rats which survived x-irradiation. J. Geront. 15, 253 (1960).
Sobel, H., S. Gabay, C. Johnson and B. Hassan: Carcass nitrogen and the hexosamine-collagen ratio of skin following starvation and cortisone administration in rats and guinea pigs. Metabolism 180 (1959).
Sobel, H., S. Gabay, E. T. Wright, I. Lichtenstein and N. H. Nelson: The influence of age upon the hexosaminecollagen ratio of dermal biopsies from men. J. Geront. 13, 128 (1958).
Sobel, H., and J. Marmorston: The effect of cortisone on the collagen and hexosamine content of the skin and femurs of one year old rats. Endocrinology 55, 21 (1954).
The possible role of the gel-f iber ratio of connective tissue in the aging process. J. Geront. 2, 1 (1956).
Sobel, H., A. Zutrauen and J. Marmorston: The collagen and hexosamine contents of the skin of normal and experimentally treated rats. Arch. Biochem. 46, 221 (1953).
Soloioxs, C. C., and J. T. Irvixg: Availability to dinitrofluorobenzene of some amino groups in human dentine and ox hide collagen. Nature (Lond.) 178, 548 (1956).
Calcification. The reaction of some hard-and soft-tissue collagens with 1-fluoro-2,4-dinitrobenzene. Biochem. J. 68, 499 (1958).
Spain, D. M., and N. Molomut: Effect of cortisone on inflammation in mice. Amer. J. clin. Path. 22, 944 (1952).
Spiro, R. G.: Studies on the biosynthesis of glucosamine in the intact rat. J. biol. Chem. 234, 742 (1959).
Srere, P. A., I. L. Chaikoff, S. S. Treitman and L. S. Burstein: The extrahepatic synthesis of cholesterol. J. biol. Chem. 182, 629 (1950).
Stainsby, G.: Viscosity of dilute gelatin solutions. Nature (Lond.) 169, 662 (1952).
Stary, Z.: Leber und Galle. In Physiologische Chemie, herausgeg. von Flaschentrager u. E. Lehnartz. Berlin-Göttingen-Heidelberg: Springer 1956.
Mucosaccharides and glycoproteins. Chemistry and Physiopathology. Ergebn. Physiol. 50, 174 (1959).
Stary, Z., u. M. Bilen Mucopolysaccharidgehalt normaler Organe. Klin. Wschr. 34, 786 (1956).
Stary, Z., U. S. Tekman Klinische und pathologische Bedeutung der Hyaluronidasen. Minch. med. Wschr. 93, 30–31 (1951).
Stary, Z., U. M. Yuvanidis: “Ober den Hexuronsäuregehalt der Serumproteine. Biochem. Z. 324, 206 (1953).
Stearns, M. L.: Studies on the development of connective tissue in transparent chambers in the rabbits ear. Amer. J. Anat. 66, 133 (1940).
Studies on the development of connective tissue in transparent chambers in the rabbits ear. Amer. J. Anat. 67, 55 (1940).
Steigleder, G. K.: Nonspecific esterases in connective tissue cells of skin. Bull. Soc. franç. Derm. Syph. 64, 554 (1957).
Steigleder, G. K., and K. Schultis: Histochemie der Haut-Esterasen. Arch. klin. exp. Derm. 205, 196 (1957).
Stein, W. H., and C. G. MILLER jr.: The composition of elastin. J. biol. Chem. 125, 599 (1938).
Stetten, M. R.: Some aspects of the metabolism of hydroxyproline; studies with the aid of isotopic nitrogen. J. biol. Chem. 181, 31 (1949).
Mechanism of the conversion of ornithine into proline and glutamic acid in vivo. J. biol. Chem. 189, 499 (1951)
Stetten, M. R., and R. Schoenheimer: The metabolism of 1(-)proline studies with the aid of deuterium and isotopic nitrogen. J. biol. Chem. 153, 113 (1944).
Stoffyn, P. J., and R. W. Jeanloz: The identification of the uronic acid component of dermatan sulfate (ß-Heparin, chondroitinsulfate B). J. biol. Chem. 235, 2507 (1960).
Stoughton, R. B., and G. Wells: A histochemical study on polysaccharides in normal and diseased skin. J. invest. Derm. 15, 37 (1950).
Strobel, H.: Die Gewebsveränderungen der Haut im Verlaufe des Lebens. Arch. Derm. Syph. (Berl.) 186, 636 (1948).
Strominger, J. L., H. M. Kalckar, J. Axelrod and E. S. Maxwell: Enzymatic oxidation of uridine diphosphate glucose (UDPG) to uridine diphosphate glucuronic acid (UDPGA). J. Amer. chem. Soc. 76, 6411 (1954).
Strominger, J. L., E. S. Maxwell, J. Axelrod and H M Kalckar: Enzymatic formation of uridine diphosphoglucuronic acid. J. biol. Chem. 224, 79 (1957).
Sutherland, G. B. B. M., K. N. Tanner and D. L. Wood: Infrared evidence for collagen structures. J. chem. Phys. 22, 1621 (1954).
Slzl’ki, S., and J. L. Strominger: Enzymatic sulfation of mucopolysaccharides in hen oviduct. I. Transfer of sulfate from 3’-phosphoadenosine 5’ phosphosulfate to mucopolysaccharides. J. biol. Chem. 235, 257 (1960).
Enzymatic sulfation of mucopolysaccharides in hen oviduct. II. Mechanisms of the reaction studied with oligosaccharides and monosaccharides as acceptors. J. biol. Chem. 235, 267 (1960).
III. Mechanism of sulfation of chondroitin and chondroitinsulfate A. J. biol. Chem. 235, 274 (1960).
Svlvén, B.: Über das Vorkommen von hochmolekularen Esterschwefelsäuren im Granulationsgewebe und bei Epithelregeneration. Acta chir. scand. 86, Suppl., 66 (1941).
Szirnai, J. A.: The connective tissue of the cock comb. Histochemical observation on the ground substances. J. Histochem. Cytochem. 4, 96 (1956).
TelkkäA., and E. Kulonen: Precipitation of polysaccharides as basis of histochemical reactions. Ann. Med. exp. Fenn. 37, 310 (1959).
Tennent, D. M . , M. E. Zanetti, W. H. Ott, G. W. Kijron and H. Siegel: Influence of crystalline elastase on experimental atherosclerosis in the chicken. Science 124, 588 (1956).
Teyssie, A. R., B. G. T. De Pogo, E. Sacerdote De Lustig and J. Scaciatti: Mucopolysaccharides of normal and tumoral fibroblasts cultured in vitro. Tex. Rep. Biol. Med. 18, 523 (1960).
Thompson, R. C.: Studies of metabolic turnover with tritium as a tracer. II. Gross studies on the rat. J. biol. Chem. 200, 731 (1953).
Thompson, R. C., and J. E. BALLOU: Studies of metabolic turnover with tritium as a tracer. IV. Matabolically inert lipide and protein fractions from the rat. J. biol. Chem. 208, 883 (1954).
Tomlin, S. G.: The structure of collagen fibers. Proc. Intern. Wool Textile Research Conf., Melbourne B 187 (1955).
Tomlin, S. G., and K. T. Turner: Electrophoretic studies of tendon collagen solutions. Biochim. biophys. Acta 26, 170 (1957).
Topper, Y. T., and M. M. Lipton: The biosynthesis of a streptococcal capsular polysaccharide. J. biol. Chem. 203, 135 (1953).
Touster, O., and V. H. Reynolds: The synthesis and properties of B-d-glucuronic acid-1 -phosphate. J. biol. Chem. 197, 863 (1952).
Tracey, M. V.: A manometric method for the estimation of milligram quantities of uronic acids. Biochem. J. 43, 185 (1948).
Trimble, H.: True sugar content of skin in diabetes. Arch. Derm. Syph. (Chicago) 25, 6 (1932).
Thimble, H. C., and B. W. Careyjr.: On the true sugar content of the skin and of muscle in diabetic and non-diabetic persons. J. biol. Chem. 90, 655 (1931).
Tuerkischer, E., and E. Wertheimer: Factors influencing deposition of glycogen in adipose tissue of the rat. J. Physiol. (Loud.) 104, 361 (1946).
Tunbridge, R. E.: Relation of elastin and collagen (morphological studies). Experientia (Basel) Suppl. No 4, 15 (1956).
Tustaxovskri, A. A.: Proteins of the skin. Biokhimiya 12, 285 (1947).
Tustanovskii, A. A., A. L. Zaides, G. V. Orlovskaya and A. N. Mikjailov: The structure of collagen. Dokl. Akad. Nauk SSSR. 97, 121 (1954).
Urbach, E., and P. Fantl: Methoden zur quantitativ-chemischen Analyse der Haut. Biochem. Z. 196, 474 (1928).
Urbach, E., and J. W. Lentz: Carbohydrate metabolism and the skin. Arch. Dermat. Syph. (Chicago) 52, 301 (1945).
Van Slyxe, D. D. and F. M. Sinex: The course of hydroxylation of lysine to form hydroxylysine in collagen. J. biol. Chem. 232, 797 (1958).
Varga, L.: Studies on hyaluronic acid prepared from the vitreous body. J. biol. Chem. 217, 651 (1955).
Varga, L . , A. Pietruszkiewicz and M. Ryan: Hyaluronic acid. I. Influence of ionic strength on the sedimentation and diffusion properties. Biochim. biophys. Acta. 32, 155 (1959).
Veis, A., and J. Cohen: The degradation of collagen. A method for the characterization of native collagen. J. Amer. chem. Soc. 76, 2476 (1954).
The role of cross linkages in the solubilization of insoluble collagen. J. physic. Chem. 62, 459 (1958).
Verzâr, F., and K. Huber: Thermal contraction of single tendon fibers from animals of different age after treatment with formaldehyde, urethan, glycerol, acetic and other substances. Gerontologia (Basel) 2, 81 (1958a).
The affinity of collagen fibers for radio-isotopes calcium-45, sodium-24, potassium-42 and iodine-131 during thermal contraction. Gerontologia (Basel) 2, 113 (1958 b).
Vinogradov, V. V., and L. P. Cheremnykh: Histochemical detection of acid mucopolysaccharides. Byull. Eksptl. Biol. i Med. 43. 124 (1957).
Viswanatha, T., and F. Irreverre: Occurrence of hydroxylysine in TRYPSIN. Biochim. Biophys. ACTA 40, 564 (1960).
Vitry, G.: La reaction metachromatique et son utilisation pour l’etude des polysaccharides. Ann Histochim. 3, 279 (1958).
Waldscro T-LErrz, E. W., G. Bretzel and L. Keller: Detection of hydroxylysine in serum protein. Naturwissenschaften 47, 254 (1960).
Wassermann, F., and A. Leydexbaum: Effect of enzymes on the reconstitution of collagenous fibrils in vitro. J. biophys. biochem. Cytol. 2, Suppl. 299 (1956).
Watson, E. M., and R. H. Pearce: The mucopolysaccharide content of the skin in localized (pretibial) myxedema. Amer. J. clin. Path. 19, 442 (1949).
Weber, G.: Vergleichende Untersuchungen über das quantitative Verhalten proteingebundener Kohlenhydrate im Blutserum bei Dermatosen. Acta derm.-venereol. (Stockh.) 38, 127 (1958).
Weber, G., O. Braun-Falco u. G. Thaesler• Zur Frage des Verhaltens proteingebundener Polysaccharide im Serum bei Dermatosen. Arch. Derm. Syph. (Berl.) 198, 634 (1954).
Derm. Wschr. 129, 561 (1954).
Weber, G., and G. Thaesler: Glucuronic acid in the blood serum during dermatoses. Minerva dean. (Torino) 34, 554 (1959).
Weissmann, B.: The transglycosylative action of testicular hyaluronidase. J. biol. Chem. 216, 783 (1955).
Weissmann, B., M. M. Rapport, A Linker and K. Meyer: Isolation of the aldobionic acid of umbilical cord hyaluronic acid. J. biol. Chem. 205, 205 (1953).
Weissmann, B., and J. Tornherm Action of purified liver extracts on a hyaluronate trisaccharide. Fed. Proc. 20, 236 (1961).
Wells, G. C., and C. Babcock: Epidermal protease. J. invest. Derm. 21, 459 (1953).
White, B. N., M. R. Shetlar, H. M. Shurley and J. A. Schilling: Wound healing: investigation of proteins, glycoproteins, and lipides of experimental wound fluid in the dog. Proc. Soc. exp. Biol. (N.Y.) 101, 353 (1959).
Windrum, G. M.: Histochemical demonstration of hyaluronic acid. A.M.A. Arch. Path. 65, 513 (1958a).
Sulfation techniques in histologic study of granulation tissue. Lab. Invest. 7, 9 (1958b).
Windrum, G. M., P. W. Kent and J. E. Eastoe: The constitution of human renal reticulin. Brit. J. exp. Path. 36, 49 (1955).
Winter, C. A., and L. Flatarer: Influence of cortisone and related steroids upon spreading effect of hyaluronidase. Fed. Proc. 9, 137 (1950).
Woessner jr., J. F., and R. J. Bouger: Connective tissue development in subcutaneously implanted polyvinyl sponge. II. Enzymic changes during development. Arch. Biochem. 92, 95 (1961).
Wolbach, S. B.: Controlled formation of collagen and reticulum: a study of the source of intercellular substance in recovery from experimental scorbutus. Amer. J. Path. 9, 689 (1933).
Wolf, G., and A. Moretti: Vitamin A and net synthesis of mucopolysaccharides. Fed. Proc. 20, 162 (1961).
Wolf, G., P. T. Varandani and B. Conner Johnson: Vitamin A and mucopolysaccharide synthesizing enzymes. Biochem. biophys. Acta 46, 59 (1961).
Wolfrom, M. L., and W. Brockneely: The uronic acid component of chondroitinsulfuric acid. J. Amer. chem. Soc. 75, 2778 (1953).
Wolfrom, M. L., and J. V. Karabinos Heparin. Hydrolytic characteristics. J. Amer. chem. Soc. 67, 679 (1945).
Wolfrom, M. L., G. M.ntgomery, J. V. Karabinos and P. Rathgeb: The structure. of heparin. J. Amer. chem. Soc. 72, 5796 (1950).
Wolfrom, M. L. and F. A. H. Rice: Uronic component of heparin. J. Amer. chem. Soc. 68, 532 (1946).
Uronic acid component of mucoitinsulfuric acid. J. Amer. chem. Soc. 69, 1833 (1947).
Wolpers, C.: Zur electronenmikroskopischen Darstellung elastischer Gewebeselemente. Klin Wschr. 23, 169 (1944).
Elektronenmikroskopische Untersuchungen zur Pathologie der kollagenen Fasern. Frankfurt. Z. Path. 61, 417 (1950).
Wood, G. C.: The stabilization of elastin by a polysaccharide. Biochem. J. 55, XXXIV (1953).
Reconstitution of elastin from a soluble protein derived from ligamentum nuchae. Biochem. J. 68, 21P (1958); 69, 539 (1958).
The formation of fibrils from collagen solutions. 2. A mechanism of collagen fibril formation. Biochem. J. 75, 598 (1960a).
The formation of fibrils from collagen solutions. 3. Effect of chondroitinsulphate and some other naturally occurring polyanions on the rate of formation. Biochem. J. 75, 605 (1960b).
Wood, G. C., and M. K. Keech The formation of fibrils from collagen solutions. I. The effect of experimental conditions: kinetic and electronmicroscope studies. Biochem. J. 75, 588 (1960).
Wynn, W., and J. Haldi Water and fat content of albino rat on high fat diet, further observations. Amer. J. Physiol. 142, 508 (1944).
Yasuda, K.: Histochemical staining of hyaluronic acid with chitosan. Okajimas Folia anat. Jap. 25, 55 (1953).
Young, E. G., and J. W. Lorimer The acid soluble collagen of cod skin Arch. Biochem. 88, 373 (1960).
Zaides, A. L., A. N. Mrrnamov, G. V. Orlovskaya and A. N. Tustanovskii: Collagen a protein consisting of several microphases and several components. Kozarstvi 9, 3 (1959).
Zantbom, V., A. A. Castellani and B. De Bernard: Uridine diphospho-glucose dehydrogenase in the metaphyseal cartilage. R. C. Ist. lomb. sci., Cl. Sci., mat. natur. 91, 14 (1957).
Zuckerman, S.: The histogenesis of tissues sensitive to oestrogens. Biol. Rev. 15, 231 (1940).
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1962 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Stary, Z. (1962). Chemistry of the Cutis. In: Keidel, WD., et al. Normale und Pathologische Physiologie der Haut I. Handbuch der Haut- und Geschlechtskrankheiten, vol 1 / 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87657-8_6
Download citation
DOI: https://doi.org/10.1007/978-3-642-87657-8_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-87658-5
Online ISBN: 978-3-642-87657-8
eBook Packages: Springer Book Archive