Skip to main content
SpringerLink
Log in

Kollagen.(Collagen.)

  • Chapter
Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrès dans la Chimie des Substances Organiques Naturelles

Zusammenfassung

Der Anlaß für unseren Arbeitskreis, sich mit dem Problem der Kollagenstruktur zu befassen, war ein äußerer. Die Kollagenfaser ist das hauptsächliche Bauelement des Bindegewebes und damit auch der Haut und des Leders. Zunächst haben wir uns — und dies gilt schon von meinem Vorgänger Max Bergmann — das Problem der chemischen Struktur des Kollagens viel zu einfach vorgestellt: Die Molekülkette, von der es zunächst offen schien, ob sie in der Länge begrenzt sei oder „fakultativ endlos“ wie die der Cellulose, sollte aufgebaut sein aus Sequenzen von je 3 bzw. 6 Aminosäuren, unter denen Glycin, Prolin und Hydroxyprolin regelmäßig wiederkehren sollten (27, 12). Im Gegensatz zu den rein spekulativen Vorstellungen über die Aminosäureanordnungen anderer Proteine, die damals auf ähnlicher Grundlage entwickelt worden sind, hat sich im Falle des Kollagens die Bergmannsche Vorstellung einer periodischen Wiederkehr kurzer, gleichartiger Sequenzen als fruchtbar erwiesen. Sie war wegleitend für die späteren 3-Ketten-Helix-Modelle nach Pauling (316), Ramachandran (334, 335, 337) und Rich und Crick (345), und sie hat in den chemischen Untersuchungen, über die unten berichtet wird, zum mindesten für die „apolaren“ Bereiche eine Bestätigung gefunden.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Literaturverzeichnis

  1. Adam, M., P. Bartl, Z. Deyl and J. Rosmus: Reaction of Gold with Collagen in vivo. Experientia 20, 203 (1964).

    CAS  Google Scholar 

  2. Adam, M., Z. Deyl and J. Rosmus: The Influence of some Anti-Inflammatory Drugs on the Structural Stability of Collagen. Conference on collagen Problems, Hluboka (CSSR), 1964; vgl. Collagen Curr. 5, 166 (1964).

    Google Scholar 

  3. Adelmann, B. und K. Kühn: Untersuchungen über nicht-kollagene Proteine des Bindegewebes. Intern. Symp. Biochem. Physiol. Connective Tissue. Lyon 1965.

    Google Scholar 

  4. Akabori, S., K. Ohno and K. Narita: On the Hydrazinolysis of Proteins and Peptides: A Method for the Characterization of Carboxyl-terminal Amino Acids in Proteins. Bull. Chem. Soc. Japan 25, 214 (1952).

    CAS  Google Scholar 

  5. Albertini, A. v. und A. Vogel: Über wirkliche Kollagenosen. Dtsch. med. Wschr. 86, 1421 (1961).

    Google Scholar 

  6. Altgelt, K., A. J. Hodge and F. O. Schmitt: Gamma Tropocollagen: A Reversibly Denaturable Collagen Macromolecule. Proc. Nat. Acad. Sei. (USA) 47, 1914 (1961).

    CAS  Google Scholar 

  7. Ambrose, E. J. and A. Elliott: Infra-red Spectra and Structure of Fibrous Proteins. Proc. Roy. Soc. (London) A 206, 206 (1951).

    Google Scholar 

  8. Anderer, F. A., H. Uhlig, E. Weber and G. Schramm: Primary Structure of the Protein of Tobacco Mosaic Virus. Nature 186, 922 (1960).

    CAS  Google Scholar 

  9. Andreeva, N. S., M. I. Millionova and Yu. N. Chirgadze: Structural Investigations of Polymers Related to Collagen. In: G. N. Ramachandran, Aspects of Protein Structure, p. 137. Academic Press. London. 1963.

    Google Scholar 

  10. Anfinsen, C. B., S. E. G. Aqvist, J. P. Cooke and B. Jönsson: A Comparative Study of the Structures of Bovine and Ovine Pancreatic Ribonuclease. J. Biol. Chem. 234, 1118 (1959).

    CAS  Google Scholar 

  11. Applequist, J.: The Helix-Coil Equilibrium in Polypeptides. J. Chem. Phys. 38, 934 (1963).

    CAS  Google Scholar 

  12. Astbury, W. T.: X-Ray Studies of Protein Structure. Cold Spring Harbor Sympos. Quant. Biol. 2, 15 (1934).

    CAS  Google Scholar 

  13. Astbury, W. T.: The Molecular Structure of the Fibres of the Collagen Group. J. Internat. Soc. Leather Trades ’ Chem. 24, 69 (1940).

    CAS  Google Scholar 

  14. Badger, R. M. und A. D. E. Pullin: The Infrared Spectrum and Structure of Collagen. J. Chem. Phys. 22, 1142 (1954).

    CAS  Google Scholar 

  15. Bailey, A. J. and A. J. Hodge: The Subunit Structure of the Tropocollagen Molecule in Relation to the Native-type Fibril and other Ordered Aggregation States. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  16. Bangle, R., Jr. 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).

    CAS  Google Scholar 

  17. Bangle, R., Jr. 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).

    CAS  Google Scholar 

  18. 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).

    CAS  Google Scholar 

  19. Bear, R. S.: The Structure of Collagen Fibrils. Adv. Protein Chem. 7, 69 (1952).

    CAS  Google Scholar 

  20. Bear, R. S.: Fibrous Proteins and their Biological Significance. Symp. Soc. Exp. Biol. 9, 97 (1955).

    Google Scholar 

  21. Bear, R. S.: The Structure of Collagen Molecules and Fibrils. J. Biophys. Biochem. Cytol. 2, 363 (1956).

    CAS  Google Scholar 

  22. Bear, R. S., O. E. Bolduan and T. P. Salo: A Model for Collagen Fibril Structure Derived from Small-angle X-Ray Diffraction. J. Amer. Leather Chem. Assoc. 46, 107 (1951).

    CAS  Google Scholar 

  23. Beek, J.: Carbohydrate Content of Collagen. J. Res. Nat. Bur. Stand. 27, 507 (1941).

    CAS  Google Scholar 

  24. Beer, M., G. B. B. M. Sutherland, K. N. Tanner and D. L. Wood: Infra-red Spectra and Structure of Proteins. Proc. Roy. Soc. (London) A 249, 147 (1959).

    Google Scholar 

  25. Beier, G. and J. Engel: The Renaturation of Soluble Collagen: Products Formed at Different Temperatures. Biochemistry (in print).

    Google Scholar 

  26. Beier, G., J. Engel und W. Grassmann: Zum Mechanismus der Bildung der Tripelhelix des Kollagens aus den denaturierten Komponenten. Tagungsbericht, Biophysiker Tagung, Wien, 1964; und Collagen Currents 5, 310 (1965).

    Google Scholar 

  27. Bekhor, I. J. and L. A. Bavetta: Actinomycin D Inhibition of Microsomal- Bound Hydroxyproline Formation in Rabbit Embryo Skin in vitro. Proc. Nat. Acad. Sei. (USA) 53, 613 (1965).

    CAS  Google Scholar 

  28. Bello, J.: On the Mechanism of Action of Neutral Salt on the Collagen-Fold. Biochemistry 2, 276 (1963).

    CAS  Google Scholar 

  29. Bensusan, H. B. and B. L. Hoyt: The Effect of Various Parameters on the Rate of Formation of Fibers from Collagen Solutions. J. Amer. Chem. Soc. 80, 719 (1958).

    CAS  Google Scholar 

  30. Bensusan, H. B. and S. O. Nielsen: The Deuterium Exchange of Peptide- Group Hydrogen Atoms during the Gelatin→Collagen-Fold Transition. Biochemistry 3, 1367 (1964).

    CAS  Google Scholar 

  31. Bergmann, M.: Complex Salts of Amino Acids and Peptides. II. Determination of l-Proline with the Aid of Rhodanilic Acid. The Structure of Gelatin. J. Biol. Chem. 110, 471 (1935).

    CAS  Google Scholar 

  32. Bergmann, M. and C. Niemann: On Blood Fibrin. A Contribution to the Problem of Protein Structure. J. Biol. Chem. 115, 77 (1936).

    CAS  Google Scholar 

  33. Bickley, H. C. and J. L. Orbison: The Effect of a Lathyrogen on Sulfate Metabolism in Culture of the Strain L Fibroblast. Lab. Invest. 13, 172 (1964).

    CAS  Google Scholar 

  34. Blumenfeld, O. O. and P. M. Gallop: The Participation of Aspartyl Residues in the Hydroxylamine - or Hydrazine-Sensitive Bonds of Collagen. Biochemistry 1, 947 (1962).

    CAS  Google Scholar 

  35. Blumenfeld, O. O., M. A. Paz, P. M. Gallop and S. Seifter: The Nature, Quantity, and Mode of Attachment of Hexoses in Ichthyocol. J. Biol. Chem. 238, 3835 (1963).

    CAS  Google Scholar 

  36. Boedtker, H. and P. Doty: The Native and Denatured States of Soluble Collagen. J. Amer. Chem. Soc. 78, 4267 (1956).

    CAS  Google Scholar 

  37. Bornstein, P., G. R. Martin and K. A. Piez: Intermolecular Cross-Linking of Collagen and the Identification of a New β-Component. Science 144, 1220 (1964).

    CAS  Google Scholar 

  38. Bornstein, P. and K. A. Piez: A Biochemical Study of Human Skin Collagen and the Relation between Intra-and Intermolecular Cross-Linking. J. Clin. Investigation 43, 1813 (1964).

    CAS  Google Scholar 

  39. Bornstein, P. and K. A. Piez: Collagen: Structural Studies Based on the Cleavage of Methionyl Bonds. Science 148, 1353 (1965).

    CAS  Google Scholar 

  40. Bowes, J. H., R. G. Elliott and J. A. Moss: The Composition of Collagen and Acid-soluble Collagen of Bovine Skin. Biochem. J. 61, 143 (1955).

    Google Scholar 

  41. Bowes, J. H. and J. A. Moss: The Reaction of Fluorodinitrobenzene with the α-and ε-Amino Groups of Collagen. Biochem. J. 55, 735 (1953).

    CAS  Google Scholar 

  42. Bradbury, E. M., R. E. Bürge, J. T. Randall and G. R. Wilkinson: The Polypeptide Chain Configurations of Native and Denatured Collagen Fibres. Disc. Faraday Soc. No. 25, 173 (1958).

    Google Scholar 

  43. Braun-Falco, O.: Über das Verhalten der interf brillären Grundsubstanz bei Skierodenrie. Dermatol. Wschr. 136, 1085 (1957).

    CAS  Google Scholar 

  44. Braunitzer, G., N. Hilschmann und R. Müller: Über den Ort des spezifischen Austausches von Aminosäuren in der β-Kette bei pathologischen menschlichen Hämoglobinen. Z. physiol. Chem. 318, 284 (1960).

    CAS  Google Scholar 

  45. Braunitzer, G., K. Hilse, V. Rudloff and N. Hilschmann: The Hemoglobins. Adv. Protein Chem. 19, 1 (1964).

    CAS  Google Scholar 

  46. Brocas, J. and F. Verzär: The Ageing of Xenopus laevis, a South African Frog. Gerontologia 5, 228 (1961); Experientia 17, 421 (1961).

    CAS  Google Scholar 

  47. Brocas, J. and F. Verzär: Measurement of Isometric Tension during Thermic Contraction as Criterion of the Biological Age of CoLagen Fibers. Gerontologia 5, 223 (1961).

    CAS  Google Scholar 

  48. Bürge, R. E. and R. D. Hynes: The Thermal Denaturation of Collagen in Solution and its Structural Implications. J. Mol. Biol. 1, 155 (1959).

    Google Scholar 

  49. Cantow, H.-J.: Streulichtmethode. In: Houben-Weyl, Methoden der organischen Chemie, 4. Aufl., Bd. III, Teil 1, S. 408. Stuttgart: GeorgeThieme. 1955.

    Google Scholar 

  50. Chvapil, M. and J. Hurych: Hydroxylation of Proline in vitro. Nature 184, “45 (1959).

    Google Scholar 

  51. Čmuchalovä, B. and M. Chvapil: The Röle of Ascorbic Acid in Collagen Biosynthesis. Conference on Collagen Problems, Hlubokä (ÖSSR), 1964; vgl. Collagen Currents 5, 165 (1964).

    Google Scholar 

  52. Cochran, W., F. H. C. Crick and V. Vand: The Structure of Synthetic Polypeptides. I. The Transform of Atoms on a Helix. Acta Crystallogr. 5, 581 (1952).

    CAS  Google Scholar 

  53. Cohen, C.: Optical Rotation and Helical Polypeptide Chain Configuration in Collagen and Gelatin. J. Biophys. Biochem. Cytol. 1, 203 (1955).

    CAS  Google Scholar 

  54. Cohen, C. und R. S. Bear: Helical Polypeptide Chain Configuration in Collagen. J. Amer. Chem. Soc. 75, 2783 (1953).

    CAS  Google Scholar 

  55. Corey, R. B. and L. Pauling: Fundamental Dimensions of Polypeptide Chains. Proc. Roy. Soc. (London) B 141, 10 (1953).

    Google Scholar 

  56. Coronado, A., E. Mardones and J. E. Allende: Isolation of Hydroxylysyl-sRNA and Hydroxyprolyl-sRNA in a Chick Embryo System. Biochem. Bio-phys. Res. Comm. 13, 75 (1963).

    CAS  Google Scholar 

  57. Coronado, A., E. Mardones, J. Celis and J. E. Allende: The Formation of Hydroxyprolyl-sRNA and Hydroxylysyl-sRNA in a Chick Embryo System. Ylth Internat. Congr. Biochem., New York 1964, Abstr. 1–35.

    Google Scholar 

  58. Cowan, P. M., S. McGavin and A. C. T. North: The Polypeptide Chain Configuration of Collagen. Nature 176, 1062 (1955).

    CAS  Google Scholar 

  59. Cowan, P. M., A. C. T. North and J. T. Randall: High-Angle X-Ray Diffraction of Collagen Fibres. In: J. T. Randall (Edit.), Nature and Structure of Collagen, p. 241. London: Butterworth. 1953.

    Google Scholar 

  60. Crick, F. H. C. and A. Rich: Structure of Polyglycine II. Nature 176, 780 (1955).

    CAS  Google Scholar 

  61. Crosby, N. T., D. G. Higgs, R. Reed, G. Stainsby and A. G. Ward: The Preparation and Properties of Solubilized Collagens. J. Soc. Leather Trades ’ Chem. 46, 152 (1962).

    CAS  Google Scholar 

  62. Crothers, D. M. and B. H. Zimm: Theory of the Melting Transition of Synthetic Polynucleotides: Evaluation of the Stacking Free Energy. J. Mol. Biol. 9, 1 (1964).

    CAS  Google Scholar 

  63. Dasler, W., R. F. Stoner and R. V. Milliser: Effect of Osteolathyrism on Soluble Collagen Fractions of Rat Connective Tissue. Metabolism 10, 883 (1961).

    CAS  Google Scholar 

  64. Delaunay, A. and S. Bazin: Mucopolysaccharides, Collagen and Nonfibrillar Proteins in Inflammation. Intern. Rev. Conn. Tiss. 2, 301 (1964).

    CAS  Google Scholar 

  65. Dick, Y. P., J. Engel and A. Nordwig: The Effect of pH on the Stability of the Collagen Fold. 2nd Meet. Fed. Europ. Biochem. Soc., Vienna, 1965.

    Google Scholar 

  66. Djerassi, C.: Optical Rotatory Dispersion. New York: McGraw-Hill. 1960.

    Google Scholar 

  67. Doty, P. and T. Nishihara: The Molecular Properties and Thermal Stability of Soluble Collagen. In: G. Stainsby (Edit.), Recent Advances in Gelatin and Glue Research, p. 92. London: Pergamon Press. 1958.

    Google Scholar 

  68. Ed man, P.: Method for Determination of the Amino Acid Sequence in Peptides. Acta Chem. Scand. 4, 283 (1950).

    CAS  Google Scholar 

  69. Edmundson, A. B.: Amino-Acid Sequence of Sperm Whale Myoglobin. Nature 205, 883 (1965).

    CAS  Google Scholar 

  70. Eichler, O.: Die Pharmakologie anorganischer Anionen. Berlin: Springer. 1950.

    Google Scholar 

  71. Engel, J.: Untersuchung des Mechanismus der Denaturierung und Renaturierung von löslichem Kollagen mit der Lichtstreuungsmethode. Z. physiol. Chem. 325, 287 (1961).

    CAS  Google Scholar 

  72. Engel, J.: Physikalisch-chemische Untersuchungen am Tropokollagen. Dissert. Univ. München, 1962.

    Google Scholar 

  73. Engel, J.: Über den Einfluß des Denaturierungsgrades und der Renaturierungs-bedingungen auf die Rückbildung kollagener Strukturen. Z. physiol. Chem. 328, 94 (1962).

    CAS  Google Scholar 

  74. Engel, J.: Investigation of the Denaturation and Renaturation of Soluble Collagen by Light Scattering. Arch. Biochem. Biophys. 97, 150 (1962).

    CAS  Google Scholar 

  75. Engel, J. und G. Beier: Die Rückbildung der Sekundär-und Tertiärstruktur denaturierter Eiweißmoleküle. Kolloid-Z. 197, 7 (1964).

    CAS  Google Scholar 

  76. Engel, J. und G. Beier: Vergleich der molekularen Daten von Tropokollagen verschiedener Kalbshäute in nativem und denaturiertem Zustand. Z. physiol. Chem. 334, 201 (1963).

    CAS  Google Scholar 

  77. Engel, J., W. Grassmann, K. Hannig und K. Kühn: Zur Bildung von Fibrillen und Long-Spacing-Segmenten aus renaturierten Tropokollagen-lösungen. Z. physiol. Chem. 329, 69 (1962).

    CAS  Google Scholar 

  78. Engel, J., J. Kurtz, E. Katchalski und A. Berger: Polymers of Tripeptides as Collagen Models. II. Conformational changes of Poly (L-prolyl-glycyl-Z,-prolyl) in Solution. J. Mol. Biol, (in print).

    Google Scholar 

  79. Engel, J., J. Kurtz, W. Traub, A. Berger and E. Katchalski: On the Mechanism of Collagen De-and Renaturation and on Conformational Changes in Related Polypeptides. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  80. Fessler, J. H.: Some Properties of Neutral-Salt-Soluble Collagen. 1. Biochem. J. 76, 452 (1960).

    CAS  Google Scholar 

  81. Fessler, J. H.: Some Properties of Neutral-Salt-Soluble Collagen. 2. Biochem. J. 76, 463 (1960).

    CAS  Google Scholar 

  82. Flory, P. J. and R. R. Garrett: Phase Transitions in Collagen and Gelatin Systems. J. Amer. Chem. Soc. 80, 4836 (1958).

    CAS  Google Scholar 

  83. Flory, P. J. and E. S. Weaver: Helix Coil Transition in Dilute Aqueous Collagen Solutions. J. Amer. Chem. Soc. 82, 4518 (1960).

    CAS  Google Scholar 

  84. Franzblau, C., S. Seifter and P. M. Gallop: The “Nondialyzable” Fraction Obtained from Ichthyocol Digested with Collagenase. Biopolymers 2, 185 (1964).

    CAS  Google Scholar 

  85. Fricke, R. and U. Hadding: Connective Tissue Proteins. Protides of tho Biological Fluids. Proc., iothColl. Bruges, 1962, p. 52. Amsterdam: Elsevier. 1963.

    Google Scholar 

  86. Fruton, J. S.: Chemical Aspects of Protein Synthesis. In: H. Neurath (Edit.), The Proteins, Vol. I, p. 190. New York: Acad. Press. 1963.

    Google Scholar 

  87. Fujii, T.: Privatmitteilung.

    Google Scholar 

  88. Fujiimoto, D. and N. Tamiya: Studies on the Hydroxylation of Lysine in vivo. Biochem. Biophys. Res. Comm. 10, 498 (1963).

    Google Scholar 

  89. Fujiimoto, D. and N. Tamiya: Studies on Collagen Metabolism with O18 as a Tracer. Biochim. Biophys. Acta 69, 559 (1963).

    Google Scholar 

  90. Fujita, Y., A. Gottlieb, B. Peterkofsky, S. Udenfriend and B. Witkop: The Preparation of eis-and trans-4-H3-L-Prolines and Their Use in Studying the Mechanism of Enzymatic Hydroxylation in Chick Embryos. J. Amer. Chem. Soc. 86, 4709 (1964).

    CAS  Google Scholar 

  91. Funakoshi, H. and H. Nöda: Estimation of the Average Length of the Inter-band Regions in Collagen Polypeptide Chain. Biochim. Biophys. Acta 86, 106 (1964).

    CAS  Google Scholar 

  92. Gallop, P. M.: Concerning some Special Structural Features of the Collagen Molecule. Biophys. J. 4, Suppl. 79 (1964).

    CAS  Google Scholar 

  93. Gallop, P. M., S. Seifter and E. Meilmann: Occurrence of “Ester-like” Linkages in Collagen. Nature 183, 1659 (1959).

    CAS  Google Scholar 

  94. Gebhardt, E. und K. Kühn: Chemische und elektronenoptische Untersuchungen über die Reaktion von Uranylacetat mit Kollagen. Z. anorg. allg. Chem. 320, 71 (1963).

    CAS  Google Scholar 

  95. Gerber, G. B. and K. I. Altman: Mechanism of Collagen Synthesis. Nature 189, 813 (1961).

    CAS  Google Scholar 

  96. Gerber, G. B., G. Gerber und K. I. Altman: Studies of Collagen Turnover in Lathyritic Rats. Arch. Biochem. Biophys. 96, 601 (1962).

    CAS  Google Scholar 

  97. Gerber, G. B., G. Gerber und K. I. Altman: Studies on the Metabolism of Tissue Proteins. I. Turnover of Collagen Labeled with Proline-U-C14 in Young Rats. J. Biol. Chem. 235, 2653 (1960).

    CAS  Google Scholar 

  98. Gerngross, O., K. Herrmann und W. Abitz: Über den Feinbau des Gelatine-micells. Biochem. Z. 228, 409 (1930).

    CAS  Google Scholar 

  99. Gibian, H.: Mucopolysaccharide und Mucopolysaccharidasen. Wien: Deuticke. 1959.

    Google Scholar 

  100. Gieseking, R.: Die Fibrillogenese in verschiedenen Bindegewebsformen des menschlichen Embryos. Beitr. Silikose-Forsch., Sonderband 4, 231 (1960).

    Google Scholar 

  101. Gieseking, R.: Elektronenoptische Befunde am embryonalen, regenerierenden und proliferierenden Bindegewebe. Beitr. Silikose-Forsch., Sonderband 4, 249 (1960).

    CAS  Google Scholar 

  102. Glegg, R. E., D. Eidinger and C. P. Leblond: Some Carbohydrate Components of Reticular Fibers. Science 118, 614 (1954).

    Google Scholar 

  103. Glimcher, M. J.: Specificity of the Molecular Structure of Organic Matrices in Mineralization. In: R. F. Sognnaes, Calcification in Biological Systems, p. 421. Washington, D. C.: Amer. Assoc. Adv. Sei. 1960.

    Google Scholar 

  104. Glimcher, M. J.: Studies on the Role of Phosphate in the Calcification of Organic Matrices. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrew (Scotland), 1964.

    Google Scholar 

  105. Glimcher, M. J., C. J. Francois, L. Richards and S. M. Krane: The Presence of Organic Phosphorus in Collagens and Gelatins. Biochem. Biophys. Acta 93, 585 (1964).

    CAS  Google Scholar 

  106. Glimcher, M. J., U. A. Friberg and P. T. Levine: The Isolation and Amino Acid Composition of the Enamel Proteins of Erupted Bovine Teeth. Biochem. J. 93, 202 (1964).

    CAS  Google Scholar 

  107. Glimcher, M. J., A. J. Hodge and F. O. Schmitt: Macromolecular Aggregation States in Relation to Mineralization. The Collagen-Hydroxyapatite System as Studied in vitro. Proc. Nat. Acad. Sei. (USA) 43, 860 (1957).

    CAS  Google Scholar 

  108. Glimcher, M. J. and S. M. Krane: The Identification of Serine Phosphate in Enamel Proteins. Biochim. Biophys. Acta 90, 477 (1964).

    CAS  Google Scholar 

  109. Gottlieb, A. and S. Udenfriend: A Hydroxyproline-Deficient Intermediate in Collagen Synthesis. Federat. Proc. (Amer. Soc. Exp. Biol.) 24, 358 (1965).

    Google Scholar 

  110. Gould, B. S. and J. F. Woessner: Biosynthesis of Collagen. The Influence of Ascorbic Acid on the Proline, Hydroxy proline, Glycine, and Collagen Content of Regenerating Guinea Pig Skin. J. Biol. Chem. 226, 289 (1957).

    CAS  Google Scholar 

  111. Grassmann, W.: Untersuchungen über Kollagen. Kolloid-Z. 77, 205 (1936).

    CAS  Google Scholar 

  112. Grassmann, W.: Unsere heutige Kenntnis des Kollagens. Leder 6, 241 (1955).

    Google Scholar 

  113. Grassmann, W.: Kollagen und Bindegewebe. Svensk Kern. Tidskr. 72, 4 (1960).

    Google Scholar 

  114. Grassmann, W.: Über Eiweißfasern (Vortrag, 24. 10. 1962). Mitt. Max-Planck-Ges. 1963, 9.

    Google Scholar 

  115. Grassmann, W., H. Endres und A. Steber: Esterbindungen in Prokollagen. Z. Naturforsch. 9 b, 513 (1954).

    Google Scholar 

  116. Grassmann, W., K. Hannig, H. Endres und A. Riedel: Zur Bindungsweise des Prolins und Hydroxy prolins. Aminosäuresequenzen des Kollagens, I. Z. physiol. Chem. 306, 123 (1956).

    CAS  Google Scholar 

  117. Grassmann, W., K. Hannig und J. Engel: Das quantitative Verhältnis zwischen α- und β-Komponente des denaturierten, löslichen Kollagens in der Ultrazentrifuge sowie Beschreibung einer schneller sedimentierenden y-Komponente. Z. physiol. Chem. 324, 284 (1961).

    CAS  Google Scholar 

  118. Grassmann, W., K. Hannig und A. Nordwig: Über die apolaren Bereiche des Kollagenmoleküls. Aminosäuresequenzen des Kollagens, VI. Z. physiol. Chem. 333, 154 (1963).

    CAS  Google Scholar 

  119. Grassmann, W., K. Hannig und M. Plöckl: Eine Methode zur quantitativen Bestimmung der Aminosäurezusammensetzung von Eiweißhydrolysaten durch Kombination von Elektrophorese und Chromatographie. Z. physiol. Chem. 299, 258 (1955).

    CAS  Google Scholar 

  120. Grassmann, W., K. Hannig und M. Schleyer: Versuche zur elektrophoreti-schen Reinigung von Trypsin. Z. physiol. Chem. 316, 71 (1959).

    CAS  Google Scholar 

  121. Grassmann, W., K. Hannig und M. Schleyer: Zur Aminosäuresequenz des Kollagens, II. Z. physiol. Chem. 322, 71 (1960).

    CAS  Google Scholar 

  122. Grassmann, W., U. Hofmann und Th. Nemetschek: Die Querstreifung von Kollagenfibrillen. Naturwiss. 39, 215 (1952).

    CAS  Google Scholar 

  123. Grassmann, W. und H. Hörmann: Endgruppenbestimmung an Kollagen und Gelatine. Z. physiol. Chem. 292, 24 (1953).

    CAS  Google Scholar 

  124. Grassmann, W., H. Hörmann und R. Hafter: Eine quantitative Bestimmung von Kohlenhydraten als Osazone. Anwendung der Methode auf Kollagen und Prokollagen. Z. physiol. Chem. 307, 87 (1957).

    CAS  Google Scholar 

  125. Grassmann, W., H. Hörmann, A. Nordwig und E. Wünsch: Zur Spezifität der Kollagenase. Z. physiol. Chem. 316, 287 (1959).

    CAS  Google Scholar 

  126. Grassmann, W., U. Hofmann, K. Kühn, H. Hörmann, H. Endres and K. Wolf: Electron Microscope and Chemical Studies of the Carbohydrate Groups of Collagen. In: R. E. Tunbridge (Edit.), Connective Tissue, p. 157. Oxford: Blackwell Sei. Publ. 1957.

    Google Scholar 

  127. Grassmann, W., J. Janicki und F. Schneider: Über die Einwirkung von Trypsin auf Kollagen. Stiasny-Festschrift, S. 74, Darmstadt: E. Roether Verl. 1937.

    Google Scholar 

  128. Grassmann, W. und K. Kühn: Abbau des Kollagens und Prokollagens mit Natriumperjodat und Phenyljodosoacetat. Z. physiol. Chem. 301, 1 (1955).

    CAS  Google Scholar 

  129. Grassmann, W. und A. Nordwig: Quantitativer kolorimetrischer Test auf Kollagenase. Z. physiol. Chem. 322, 267 (1960).

    CAS  Google Scholar 

  130. Grassmann, W., A. Nordwig und H. Hörmann: Über den Bau der apolaren Bereiche der Kollagenfaser: Abbau mit Kollagenase. Aminosäuresequenzen des Kollagens, III. Z. physiol. Chem. 323, 48 (1961).

    CAS  Google Scholar 

  131. Grassmann, W., A. Riedel und Th. Altenschöpfer: Chemische Veränderungen beim Übergang von gekälkter Haut in Gelatine. Kolloid-Z. 186, 50 (1962).

    CAS  Google Scholar 

  132. Grassmann, W. und K. Riederle: Über die Konstitution des Glutokyrins. 3. Mitt. zur Kenntnis des Kollagens. Biochem. Z. 284, 177 (1936).

    CAS  Google Scholar 

  133. Grassmann, W. und H. Schleich: Über den Kohlenhydratgehalt des Kollagens. 2. Mitt. zur Kenntnis des Kollagens. Biochem. Z. 277, 320 (1935).

    CAS  Google Scholar 

  134. Grassmann, W., F. Schneider und J. Truppke: Eiweißstoffe und ihre Abbaustufen. In: Flaschenträger und Lehnartz, Physiologische Chemie, Band I, S. 484, insb. S. 661, Abb. 72. Heidelberg: Springer-Verlag. 1951.

    Google Scholar 

  135. Grassmann, W., O. V. Schoenebeck und G. Auerbach: Über die enzymatische Spaltbarkeit der Prolinpeptide, II. Z. physiol. Chem. 210, 1 (1932).

    CAS  Google Scholar 

  136. Grassmann, W. und P. Stadler: Gerbversuche an Kollagenfibrillen. Leder 12, 290 (1961).

    CAS  Google Scholar 

  137. Grassmann, W., L. Strauch und A. Nordwig: Reinigung von Köllagenase, II. Z. physiol. Chem. 332, 325 (1963).

    CAS  Google Scholar 

  138. Green, N. M. and D. A. Lowther: Formation of Collagen Hydroxyproline in vitro. Biochem. J. 71, 55 (1959).

    Google Scholar 

  139. Greenberg, J., L. Fishman and M. Levy: Positions of Amino Acids in Mixed Peptides Produced from Collagen by the Action of Collagenase. Biochemistry 3, 1826 (1964).

    CAS  Google Scholar 

  140. Gries, G. und J. Lindner: Untersuchungen über den Kollagenabbau bei akuten Entzündungen. Z. Rheumaforschg. 20, 122 (1961).

    CAS  Google Scholar 

  141. Grimm, L. und W. Grassmann: Das enzymchemische Verhalten der Lysyl- Prolin-Bindung und der Lysyl-Hydroxyprolin-Bindung. Ein Beitrag zur Spezifität des Trypsins. Z. physiol. Chem. 337, 161 (1964).

    CAS  Google Scholar 

  142. Gross, E. and B. Witkop: Nonenzymatic Cleavage of Peptide Bonds: The Methionine Residues in Bovine Pancreatic Ribonuclease. J. Biol. Chem. 237, 1856 (1952).

    Google Scholar 

  143. Gross, J.: Studies on the Formation of Collagen. III. Time-dependent Solubility Changes of Collagen in Vitro. J. Exp. Medicine 108, 215 (1958).

    CAS  Google Scholar 

  144. Gross, J.: Studies on the Formation of Collagen. II. The Influence of Growth Rate on Neutral Salt Extracts of Guinea Pig Dermis. J. Exp. Medicine 107, 265 (1958).

    CAS  Google Scholar 

  145. Gross, J.: Studies on the Biology of Connective Tissues: Remodelling of Collagen in Metamorphosis. Medicine 43, 291 (1964).

    CAS  Google Scholar 

  146. Gross, J., B. Dumsha and N. Glazer: Comparative Biochemistry of Collagen. Some Amino Acids and Carbohydrates. Biochim. Biophys. Acta 30, 293 (1958).

    CAS  Google Scholar 

  147. Gross, J., J. H. Highberger and F. O. Schmitt: Some Factors Involved in the Fibrogenesis of Collagen in vitro. Proc. Soc. Exp. Biol. Med. 80, 462 (1952).

    CAS  Google Scholar 

  148. Gross, J., J. H. Highberger and F. O. Schmitt: Collagen Structures Considered as States of Aggregation of a Kinetic Unit. The Tropocollagen Particle. Proc. Nat. Acad. Sei. (USA) 40, 679 (1954).

    CAS  Google Scholar 

  149. Gross, J., J. H. Highberger and F. O. Schmitt: Extraction of Collagen from Connective Tissue by Neutral Salt Solutions. Proc. Nat. Acad. Sei. (USA) 41, 1 (1955).

    CAS  Google Scholar 

  150. Gross, J. and D. Kirk: The Heat Precipitation of Collagen from Neutral Salt Solutions: Some Rate-Regulating Factors. J. Biol. Chem. 233, 355 (1958).

    CAS  Google Scholar 

  151. Gross, J. and C. M. Lapiere: Collagenolytic Activity in Amphibian Tissues: A Tissue Culture Assay. Proc. Nat. Acad. Sei. (USA) 48, 1014 (1962).

    CAS  Google Scholar 

  152. Gross, J. and G. R. Martin: Alternations of Cross Linking in Collagen in Experimental Lathyrism. 141th Meeting Amer. Chem. Soc., March 1962, Abstracts 2C.

    Google Scholar 

  153. Gross, J., Y. Nagai, C. M. Lapiere, G. Usuku, H. C. Grillo and A. Z. Eisen: Animal Collagenase and Collagen Metabolism. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  154. Günther, Th. und P. M. Carsten: Über die Löslichkeit von Kollagen in Abhängigkeit von Nebennierenrindenhormonen. Naturwiss. 48, 699 (1961).

    Google Scholar 

  155. Gustavson, K. H.: The Chemistry and Reactivity of Collagen, p. 225. New York: Academic Press. 1956.

    Google Scholar 

  156. Gustavson, K. H.: The Chemistry of Tanning Processes, p. 246. New York: Academic Press. 1956.

    Google Scholar 

  157. Gustavson, K. H.: Hydrothermal Stability and Intermolecular Organization of Collagens from Mammalian and Teleost Skins. Svensk Kem. Tidskr. 65, 70 (1953).

    CAS  Google Scholar 

  158. Gustavson, K. H.: The Function of Hydroxyproline in Collagens. Nature 175, 70 (1955).

    CAS  Google Scholar 

  159. Hafter, R.: Zur Fibrillenbildung des Kollagens, II. Mitt. Das Verhalten von Tropokollagen und Gelatine unter isoelektrischen Bedingungen. Leder 15, 237 (1964).

    CAS  Google Scholar 

  160. Hafter, R. und H. Hörmann: Der Einfluß von Pepsin auf die Struktur und die faserbildenden Eigenschaften von Kollagen. Z. physiol. Chem. 330, 169 (1963).

    CAS  Google Scholar 

  161. Hall, C. E. and P. Doty: A Comparison Between the Dimensions of Some Macromolecules Determined by Electron Microscopy and by Physical Chemical Methods. J. Amer. Chem. Soc. 80, 1269 (1958).

    CAS  Google Scholar 

  162. Hall, C. E., M. A. Jakus and F. O. Schmitt: Electron Microscope Observations of Collagen. J. Amer. Chem. Soc. 64, 1234 (1942).

    CAS  Google Scholar 

  163. Hamaguchi, K. and E. P. Geiduschek: The Effect of Electrolytes on the Stability of the Deoxyribonucleate Helix. J. Amer. Chem. Soc. 84, 1329 (1962).

    CAS  Google Scholar 

  164. Hannig, K.: Eine Apparatur zur kontinuierlichen Ablenkungselektrophorese auf Filtrierkarton bei gleichzeitiger Anwendung hoher Feldstärken. Z. physiol. Chem. 311, 63 (1958).

    CAS  Google Scholar 

  165. Hannig, K.: Investigations on the Sequence of Amino Acid Residues in Collagen. Federat. Proc. (Amer. Soc. Exp. Biol.) 19, 1 (1960).

    Google Scholar 

  166. Hannig, K. und J. Engel: Physikalisch-chemische Untersuchungen an Tropo-kollagenlösungen. Leder 12, 213 (1961).

    CAS  Google Scholar 

  167. Hannig, K., M. R. Nagamani und G. Beier: Unveröffentlicht.

    Google Scholar 

  168. Harkness, R. D., A. M. Marko, H. M. Muir and A. Neuberger: The Metabolism of Collagen and other Proteins of the Skin of Rabbits. Biochem. J. 56, 558 (1954).

    CAS  Google Scholar 

  169. Harms, H.: Elastinfärbung mit Orcein. In: Handbuch der Farbstoffe für die Mikroskopie, Teil II, S. 160. Kamp-Lintfort: Staufen Verl. 1957.

    Google Scholar 

  170. Harrington, W. F.: On the Arrangement of the Hydrogen Bonds in the Structure of Collagen. J. Mol. Biol. 9, 613 (1964).

    CAS  Google Scholar 

  171. Harrington, W. F. and P. H. v. Hippel: Formation and Stabilization of the Collagen-Fold. Arch. Biochem, Biophys. 92, 100 (1961).

    CAS  Google Scholar 

  172. Harrington, W. F. and J. Kurtz: The Effect of LiBr on the Configuration of Poly-L-proline. Collagen Currents 4, No. 11, 34 (1964).

    Google Scholar 

  173. Hartley, B. S.: Amino-Acid Sequence of Bovine Chymotrypsinogen-A. Nature 201, 1284 (1964).

    CAS  Google Scholar 

  174. Hashimoto, Y., T. Yamano and H. S. Mason: An Electron Spin Resonance Study of Microsomal Electron Transport. J. Biol. Chem. 237, 3843 (1962).

    CAS  Google Scholar 

  175. Haurowitz, F.: The Chemistry and Function of Proteins, p. 394. New York: Academic Press. 1963.

    Google Scholar 

  176. Hausmann, E. and W. F. Neuman: Conversion of Proline to Hydroxyproline and its Incorporation into Collagen. J. Biol. Chem. 236, 149 (1961).

    CAS  Google Scholar 

  177. Heidrich, H. G. and L. Wynston: A Report on the Presence of a Third Alpha Component in Calf and Rat Skin Tropocollagen. Z. physiol. Chem. 341, 1 (1965).

    Google Scholar 

  178. Heringa, G. C. und N. H. Kolkmeijer: Verh. Koninkl. Akad. Wetenschap, Amsterdam, Afdeel Natuurk. 29, 1029 (1926).

    Google Scholar 

  179. Herzog, R. O. und H. W. Gonnell: Weitere Untersuchungen an Naturstoffen und biologischen Strukturen mittels Röntgenstrahlen. Naturwiss. 12, 1153 (1924).

    CAS  Google Scholar 

  180. Herzog, R. O. und H. W. Gonnell: Über Kollagen. Ber. dtsch. chem. Ges. 58, 2228 (1925).

    Google Scholar 

  181. Herzog, R. O. und H. W. Gonnell: Über Kollagen. Collegium (Darmstadt) 1926, 189.

    Google Scholar 

  182. Herzog, R. O. und W. Jancke: Notiz über Röntgendiagramm des Kollagens (Faserperiode). Z. physik. Chemie B12, 228 (1931).

    Google Scholar 

  183. Heyns, K. und G. Legler: Über Proteine und deren Abbauprodukte, XVI. Über die Spezifität der Kollagenase aus Cl. histolyticum und ihre Anwendung zur Ermittlung der Primärstruktur des Kollagens. Z. physiol. Chem. 315, 288 (1959).

    CAS  Google Scholar 

  184. Highberger, J. H., J. Gross and F. O. Schmitt: Electron Microscope Observations of Certain Fibrous Structures Obtained from Connective Tissue Extracts. J. Amer. Chem. Soc. 72, 3321 (1950).

    CAS  Google Scholar 

  185. Highberger, J. H., J. Gross and F. O. Schmitt: The Interaction of Mucoprotein with Soluble Collagen; an Electron Microscope Study. Proc. Nat. Acad. Sei. (USA) 37, 286 (1951).

    CAS  Google Scholar 

  186. Hippel, P. H. v., P. M. Gallop, S. Seifter and R. S. Cunningham: An Enzymatic Examination of the Structure of the Collagen Macromolecule. J. Amer. Chem. Soc. 82, 2774 (1960).

    Google Scholar 

  187. Hippel, P. H. v. and W. F. Harrington: The Structure and Stabilization of the Collagen Macromolecule. Proc., Sympos. Protein Structure and Function, Brookhaven Nat. Lab., 1960, No. 13, p. 213.

    Google Scholar 

  188. Hippel, P. H. v. and K. Y. Wong: The Collagen ⇄ Gelatin Phase Transition. II, Shape of the Melting Curves and Effect of Chain Length. Biochemistry 2, 1399 (1963).

    CAS  Google Scholar 

  189. Hippel, P. H. v. and K. Y. Wong: The Collagen ⇄ Gelatine Phase Transition. I. Further Studies of the Effects of Solvent Environment and Polypeptide Chain Composition. Biochemistry 2, 1387 (1963).

    CAS  Google Scholar 

  190. Hippel, P. H. v. and K. Y. Wong: The Effect of Ions on the Kinetics of Formation and the Stability of the Collagen-Fold. Biochemistry 1, 664 (1962).

    Google Scholar 

  191. Hippel, P. H. v. and K. Y. Wong: Neutral Salts: The Generality of their Effects on the Stability of Macromolecular Conformations. Science 145, 577 (1964).

    Google Scholar 

  192. Hodge, A. J., J. H. Highberger, G. G. J. Deffner and F. O. Schmitt: The Effects of Proteases on the Tropocollagen Macromolecule and on its Aggregation Properties. Proc. Nat. Acad. Sei. (USA) 46, 197 (1960).

    CAS  Google Scholar 

  193. Hodge, A. J. and J. A. Petruska: Recent Studies with the Electron Microscope on Ordered Aggregates of the Tropocollagen Macromolecule. In: G. N. Ramachandran (Edit.), Aspects of Protein Structure, p. 289. London-New York: Academic Press. 1963.

    Google Scholar 

  194. Hodge, A. J., J. A. Petruska and A. J. Bailey: The Subunit Structure of the Tropocollagen Molecule and its Relation to Various Ordered Aggregation States. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  195. Hodge, A. J. and F. O. Schmitt: Interaction Properties of Sonically Fragmented Collagen Macromolecules. Proc. Nat. Acad. Sei. (USA) 44, 418 (1958).

    CAS  Google Scholar 

  196. Hodge, A. J. and F. O. Schmitt: The Charge Profile of the Tropocollagen Macromolecule and the Packing Arrangement in Native-Type Collagen Fibrils. Proc. Nat. Acad. Sei. (USA) 46, 186 (1960).

    CAS  Google Scholar 

  197. Hofmann, U., Th. Nemetschek und W. Grassmann: Über die Querstreifung von Kollagenfibrillen und ihre Veränderung im Elektronenmikroskop. Z. Naturforsch. 7 b, 509 (1952).

    Google Scholar 

  198. Hörmann, H.: Chemische Untersuchungen über die Kohlenhydratgrup-pierung des Kollagens. Leder 11, 173 (1960).

    Google Scholar 

  199. Hörmann, H.: Die Kohlenhydrate des Bindegewebes. Beitr. Silikoseforsch., Sonderband II, 619(1956).

    Google Scholar 

  200. Hörmann, H.: Zur Frage der Quervernetzung von Kollagen. Leder 13, 79 (1962).

    Google Scholar 

  201. Hörmann, H.: Chemical Methods for the Conversion of Insoluble Collagen into Tropocollagen. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  202. Hörmann, H.: Untersuchungen zur quantitativen Bestimmung von Carbonsäureestern mit Hydroxylamin. Monatsh. Chemie 96, 37 (1965).

    Google Scholar 

  203. Hörmann, H., K. Dorfner und M. Jellinek: Unveröffentlicht.

    Google Scholar 

  204. Hörmann, H. und R. Hafter: Zur Fibrillenbildung des Kollagens. Leder 14, 293 (1963).

    Google Scholar 

  205. Hörmann, H. and K. Th. Joseph: The Presence of Acetyl Groups in Collagen. Biochim. Biophys. Acta 100, 598 (1965).

    Google Scholar 

  206. Hörmann, H., K. Th. Joseph und M. v. Wilm: Acetylierte Aminoendgruppen in den Untereinheiten der Peptidketten des Kollagens. Z. physiol. Chem. 341, 284 (1965).

    Google Scholar 

  207. Hörmann, H., A. Riedel, Th. Altenschöpfer und M. Klenk: Chemische Veränderungen der Haut bei langdauerndem Äscher. Leder 12, 175 (1961).

    Google Scholar 

  208. Hörmann, H. und M. v. Wilm: Kollagensegmente mit symmetrischer Querstreifung. Naturwiss. 51, 464 (1964).

    Google Scholar 

  209. Hörmann, H., K. Th. Joseph und M. v. Wilm: Symp. Lyon 1965.

    Google Scholar 

  210. Houck, J. C.: Effect of Cortisol and Salicylate upon the Connective Tissue. Amer. J. Pathol. 41, 365 (1962).

    CAS  Google Scholar 

  211. Houck, J. C., E. R. Goldstein and Y. M. Patel: Collagenolytic Activity of the Connective Tissue. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  212. Houck, J. C. and R. A. Jacob: Connective Tissue. VII. Factors Inhibiting the Dermal Chemical Response to Cortisol. Proc. Soc. Exp. Biol. Med. 113, 692 (1963).

    CAS  Google Scholar 

  213. Huggins, M. L.: The Structure of Fibrous Proteins. Chem. Rev. 32, 195 (1943).

    CAS  Google Scholar 

  214. Huggins, M. L.: The Structure of Collagen. Proc. Nat. Acad. Sei. (USA) 43, 209 (1957).

    CAS  Google Scholar 

  215. Hurych, J.: Biosynthesis of Collagen. Hydroxylation of Proline in vitro. Collagen Currents 4, No. 5, p. 34 (1963).

    Google Scholar 

  216. Hurych, J.: C. Sc. Dissert., Karlsuniversität Prag, 1965.

    Google Scholar 

  217. Hurych, J. and M. Chvapil: Influence of Chelating Agents on the Biosynthesis of Collagen. Biochim. Biophys. Acta 97, 361 (1965).

    CAS  Google Scholar 

  218. Jackson, D. S.: Connective Tissue Growth Stimulated by Carrageenin. 1. The Formation and Removal of Collagen. Biochem. J. 65, 277 (1957).

    CAS  Google Scholar 

  219. Jackson, D. S.: Metabolic Studies: Turnover of α- and β-Chains. 141st Meeting Amer. Chem. Soc., Washington D. C. 1962, Abstr. p. 8C.

    Google Scholar 

  220. Jackson, D. S., D. Watkins and A. Winkler: Formation of sRNA-Hydroxy-proline in Chick-Embryo and Wound Granulation Tissue. Biochim. Biophys. Acta 87, 152 (1964).

    CAS  Google Scholar 

  221. Jackson, S. F.: Structural Problems Associated with the Formation of Collagen Fibrils in vivo. In: R. E. Tunbridge et al. (Edit.), Connective Tissue, p. 77. Oxford: Blackwell Sei. Publ. 1957.

    Google Scholar 

  222. Jasin, H. E., C. W. Fink, W. Wise and M. Ziff: Relationship between Urinary Hydroxyproline and Growth. J. Clin. Investigation 41, 1928 (1962).

    CAS  Google Scholar 

  223. Jeffrey, J. J. and G. R. Martin: Ascorbic Acid Dependent Synthesis of Collagen by Embryonic Chick Tibia Grown in Tissue Culture. Vlth Intern. Congr. Biochem., New York 1964, Abstr. 1–90.

    Google Scholar 

  224. Joseph, K. Th. and S. M. Bose: N-Terminal Amino Acids of the Constituent Proteins of Hides and Skins. Bull. Central Leather Res. Inst. 4, No. 9 (1958).

    Google Scholar 

  225. Josse, J. and W. F. Harrington: Role of Pyrrolidine Residues in the Structure and Stabilisation of Collagen. J. Mol. Biol. 9, 269 (1964).

    CAS  Google Scholar 

  226. Juva, K. and D. J. Prockop: Puromycin Inhibition of Collagen Synthesis as Evidence for Ribosomal or Post-ribosomal Site for the Hydroxylation of Proline. Biochim. Biophys. Acta 91, 174 (1964).

    CAS  Google Scholar 

  227. Karnovsky, M. J. and M. L. Karnovsky: Metabolic Effects of Lathyrogenic Agents on Cartilage in vivo and in vitro. J. Exp. Medicine 113, 381 (1961).

    CAS  Google Scholar 

  228. Katchalski, E., A. Berger and J. Kurtz: Behaviour in Solution of Polypeptides Related to Collagen. In: G. N. Ramachandran (Edit.), Aspects of Protein Structure, p. 205. London-New York: Academic Press. 1963.

    Google Scholar 

  229. Katchalsky, A. und A. Oplatka: Persönliche Mitteilung.

    Google Scholar 

  230. Katz, J. R.: Zur Polymorphie der hochmolekularen Substanzen. III. Die Mutarotation der Gelatine im Zusammenhang mit der Änderung des Röntgenspektrums beim Gelatinieren. Ree. trav. chim. Pays-Bas 51, 835 (1932).

    CAS  Google Scholar 

  231. 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, 27 (1954).

    Google Scholar 

  232. Keech, M. K. and R. Reed: Enzymic Elucidation of the Relation between Collagen and Elastin: An Electron-microscopic Study. Ann. Rheum. Diseases 16, 35 (1957).

    CAS  Google Scholar 

  233. Keil, B. and F. Šorm: On the Structure of Chymotrypsinogen A. ist Meeting Fed. Europ. Biochem. Soc., London 1964, Abstr. D-5.

    Google Scholar 

  234. Klemperer, P., A. D. Pollack and G. Baehr: Pathology of Disseminated Lupus erythematodes. Amer. Med. Assoc. Arch. Pathol. 32, 596 (1941).

    Google Scholar 

  235. Konno, K. and T. Tetsuka: The Isotopic Studies on the Conversion of Proline to Hydroxyproline. J. Biochemisty (Tokyo) 52, 466 (1962).

    CAS  Google Scholar 

  236. Konno, K. and T. Tetsuka: Studies on the Connective Tissue. III. Biosynthesis of Collagen by the Granuloma Tissue in vitro. J. Biochem. (Tokyo) 56, 581 (1964).

    CAS  Google Scholar 

  237. Körting, G. W., H. Holzmann und K. Kühn: Biochemische Bindegewebs-untersuchungen in Analogie zum Sklerodermie-Problem. Med. Welt Nr. 34, 1751 (1964).

    Google Scholar 

  238. Kowalewski, K. and M. A. Emery: Effect of Lathyrus Factor and of an Anabolic Steroid on Healing of Fractures in Rats, Studied by S85 Uptake Method. Acta Endocrinol. 34, 317 (1960).

    CAS  Google Scholar 

  239. Kratky, O. und A. Sekora: Die Auffindung von großen Netzebenenabständen bei Känguruh-Schwanzsehne. Makromolek. Chem. [3] 1, 113 (1944).

    Google Scholar 

  240. Kretsinger, R. H., G. Manner, B. S. Gould and A. Rich: Synthesis of Collagen on Polyribosomes. Nature 202, 438 (1964).

    CAS  Google Scholar 

  241. Kroner, T. D., W. Tabroff and J. J. MacGarr: Peptides Isolated from a Partial Hydrolysate of Steer Hide Collagen. J. Amer. Chem. Soc. 75, 4084 (1953).

    CAS  Google Scholar 

  242. Kroner, T. D., W. Tabroff and J. J. MacGarr: Peptides Isolated from a Partial Hydrolysate of Steer Hide Collagen. II. Evidence for the Prolyl-Hydroxyproline Linkage in Collagen. J. Amer. Chem. Soc. 77, 3356 (1955).

    CAS  Google Scholar 

  243. Kühn, K.: Über die Ausbildung einer hochunterteilten Querstreifung des Kollagens nach Gerben mit Phosphorwolframsäure und mit basischen Chromsalzlösungen. Leder 9, 217 (1958).

    Google Scholar 

  244. Kühn, K.: Über den Ursprung des Querstreifungsmusters bei Kollagen. Leder n, 110(1960).

    Google Scholar 

  245. Kühn, K.: Die End-an-End-Verknüpfung der Tropokollagenmoleküle. Leder 13, 86 (1962).

    Google Scholar 

  246. Kühn, K.: Investigations of the Renaturation of Tropocollagen. In: G. N. Rama-chandran (Edit.), Aspects of Protein Structure, p. 279. London: Academic Press. 1963.

    Google Scholar 

  247. Kühn, K., M. Durruti, P. Iwangoff, F. Hammerstein, K. Stecher, H. Holz-mann, und G. W. Körting: Untersuchungen über den Stoffwechsel des Kollagens, I. Der Einbau von [14C]-Glycin in Kollagen bei lathyritischen Ratten. Z. physiol. Chem. 336, 4 (1964).

    Google Scholar 

  248. Kühn, K. und M. Eggl: Ein kollagenolytischer Effekt bei kombinierter Einwirkung von Pronase, Pepsin und Trypsin auf Kollagen (in Vorbereitung).

    Google Scholar 

  249. Kühn, K., J. Engel, B. Zimmermann and W. Grassmann: Renaturation of Soluble Collagen. III. Reorganization of Native Collagen Molecules from Completely Separated Units. Arch. Biochem. Biophys. 105, 387 (1964).

    Google Scholar 

  250. Kühn, K. und P. Fietzek: Die Einwirkung von Proteasen auf unlösliches Kollagen (in Vorbereitung).

    Google Scholar 

  251. Kühn, K., P. Fietzek und J. Kühn: Die Einwirkung von proteolytischen Enzymen auf unlösliches Kollagen. Naturwiss. 50, 444 (1963).

    Google Scholar 

  252. Kühn, K. und E. Gebhardt: Chemische und elektronenoptische Untersuchungen über die Reaktion von Chrom(III).komplexen mit Kollagen. Z. Naturforsch. 15b, 23 (1960).

    Google Scholar 

  253. Kühn, K. und E. Gebhardt: Chemische und elektronenoptische Untersuchungen über die Reaktion von basischen Chrom(III).komplexen mit Kollagen. Leder 11, 147 (1960).

    Google Scholar 

  254. Kühn, K., W. Grassmann und U. Hofmann: Über die Bildung der Phosphorwolframsäure in Kollagen. Naturwiss. 44, 538 (1957).

    Google Scholar 

  255. Kühn, K., W. Grassmann und U. Hofmann: Die elektronenmikroskopische,, Anfärbung“ des Kollagens und die Ausbildung einer hochunterteilten Querstreifung. Z. Naturforsch. 13b, 154 (1958).

    Google Scholar 

  256. Kühn, K., W. Grassmann und U. Hofmann: Über die Bildung der Kollagenfibrillen aus gelöstem Kollagen und die Funktion der kohlenhydrathaltigen Begleitkomponenten. Z. Naturforsch. 14 b, 436 (1959).

    Google Scholar 

  257. Kühn, K., W. Grassmann und U. Hofmann: Über den Aufbau der Kollagenfibrillen aus Tropokollagenmolekeln. Naturwiss. 47, 258 (1960).

    Google Scholar 

  258. Kühn, K., F. Hammerstein, K. Stecher, M. Durruti, H. Holzmann und G. W. Korting: Untersuchungen über den Stoffwechsel des Kollagens. IV. Der Einbau von C14-Glycin in Kollagen bei mit Resochin behandelten Ratten, (in Vorbereitung).

    Google Scholar 

  259. Kühn, K., K. Hannig und H. Hörmann: Die Einwirkung von Trypsin und Pepsin auf natives Kollagen. Leder 12, 237 (1961).

    Google Scholar 

  260. Kühn, K., U. Hofmann und W. Grassmann: Über die Verteilung der basischen Aminosäuren in der Tropokollagenmolekel. Naturwiss. 46, 512 (1959).

    Google Scholar 

  261. Kühn, K., U. Hofmann und W. Grassmann: Über die Verteilung der sauren Aminosäuren in der Tropokollagenmolekel. Naturwiss. 47, 15 (1960).

    Google Scholar 

  262. Kühn, K., U. Hofmann, W. Grassmann und E. Gebhardt: Veränderung der Intensität der Querstreifen des Kollagens durch Einlagerung von Phosphorwolframsäure. Naturwiss. 45, 521 (1958).

    Google Scholar 

  263. Kühn, K., H. Holzmann und G. W. Körting: Quantitative Bestimmungen der löslichen Kollagenvorstufen nach Anwendung einiger Bindegewebsthera-peutica. Naturwiss. 49, 134 (1962).

    Google Scholar 

  264. Kühn, K., P. Iwangoff, F. Hammerstein, K. Stecher, M. Durruti, H. Holzmann und G. W. Körting: Untersuchungen über den Stoffwechsel des Kollagens, II. Der Einbau von [14C]-Glycin in Kollagen bei mit Prednison behandelten Ratten. Z. physiol. Chem. 337, 249 (1964).

    Google Scholar 

  265. Kühn, K., J. Kühn und K. Hannig: Die Einwirkung von Trypsin auf gelöstes Kollagen. Z. physiol. Chem. 326, 50 (1961).

    Google Scholar 

  266. Kühn, K., J. Kühn und G. Schuppler: Kollagenfibrillen mit anormalem Querstreifungsmuster. Naturwiss. 51, 337 (1964).

    Google Scholar 

  267. Kühn, K., G. Schuppler und J. Kühn: Veränderungen im Verhalten des Kol-lagens mit zunehmender Reinigung und nach Behandlung mit proteolytischen Enzymen. Z. physiol. Chem. 338, 10 (1964).

    Google Scholar 

  268. Kühn, K., K. Stecher, P. Iwangoff, F. Hammerstein, M. Durruti, H. Holzmann and G.W. Korting: Studies on the Metabolism of Collagen, III. The Incorporation of [14C]-Glycine into the Collagen of Rats Treated with Progesterone. Biochem. Z. (in print).

    Google Scholar 

  269. Kühn, K., Ch. Tkocz, B. Zimmermann and G. Beier: Long-Spacing-Segments from Renatured ai-Subunits of Collagen. Nature (in print).

    Google Scholar 

  270. Kühn, K. und E. Zimmer: Eigenschaften des Tropokollagenmoleküls und deren Bedeutung für die Fibrillenbildung. Z. Naturforsch. 16 b, 648 (1961).

    Google Scholar 

  271. Kühn, K. und E. Zimmer: Über die Anordnung der Tropokollagenmolekeln in den Long-Spacing-Kollagenfibrillen. Naturwiss. 48, 219 (1961).

    Google Scholar 

  272. Kühn, K. und E. Zimmer: Über eine neue Form der Long-Spacing-Fibrillen des Kollagens. Naturwiss. 48, 220 (1961).

    Google Scholar 

  273. Kühn, K., E. Zimmer, P. Waykole und P. Fietzek: Die Wirkung von Alkali auf Kollagen. Die Änderung des Ladungsmusters der Tropokollagenmoleküle sowie die Spaltung der intra-und intermolekularen Bindungen. Z. physiol. Chem. 333, 209 (1963).

    Google Scholar 

  274. Kühn, K. and B. Zimmermann: Renaturation of Soluble Collagen. IV. Regeneration of Native Collagen Molecules from α-Subunits. Arch. Biochem. Biophys. 109, 421 (1965).

    Google Scholar 

  275. Kühn, K., B. Zimmermann und Ch. Tkocz: Elektronenmikroskopische Beiträge zur chemischen Struktur des Kollagens. Sitz. Ber. Bayr. Akad. Wissensch. (4. Juli 1965 ).

    Google Scholar 

  276. Kühne, W.: Unters, physiol. ehem. Inst. Heidelberg 1, 219 (1877).

    Google Scholar 

  277. Küntzel, A. und F. Prakke: Morphologie und Feinbau der kollagenen Faser. Biochem. Z. 267, 243 (1933).

    Google Scholar 

  278. Lakshmanan, B. R., C. Ramakrishnan, V. Sasisekharan and Y. T. Thatha-Chari: X-Ray Diffraction Pattern of Collagen and the Fourier Transform of the Collagen Structure. In: N. Ramanathan (Edit.), Collagen, p. 117. London: Interscience Publ. 1962.

    Google Scholar 

  279. Lamport, D. T. A.: Oxygen Fixation into Hydroxyproline of Plant Cell WalJ Protein. J. Biol. Chem. 238, 1438 (1963).

    CAS  Google Scholar 

  280. Lamport, D. T. A.:Hydroxyproline Biosynthesis: Loss of Hydrogen during the Hydroxylation of Proline. Nature 202, 293 (1964).

    CAS  Google Scholar 

  281. Levene, C. I. and J. Gross: Alterations in State of Molecular Aggregation of Collagen Induced in Chick Embryos by β-Aminopropionitrile (Lathyrus- Factor). J. Exp. Medicine no, 771 (1959).

    Google Scholar 

  282. Levine, M.: Conversion of Proline to Hydroxyproline in Rat Skin, in vitro. 46th Annu. Meeting, Federat. Amer. Soc. Exp. Biol., Atlantic City 1962, Abstr. No. 120.

    Google Scholar 

  283. Levy, M., L. Fishman and G. Cabrera: ε-Amino Group of Lysine, a Branch Point in Collagen Structure. Federat. Proc. (Amer. Soc. Exp. Biol.) 19, 343 (1960).

    Google Scholar 

  284. Lifzson, S. and A. Roig: On the Theory of Helix-Coil Transition in Polypeptides. J. Chem. Phys. 34, 1963 (1961).

    CAS  Google Scholar 

  285. Lowther, D. A., N. M. Green and J. A. Chapman: Morphological and Chemical Studies of Collagen Formation. II. Metabolic Activity of Collagen Associated with Subcellular Fractions of Guinea Pig Granulomata. J. Biophys. Biochem. Cytol. 10, 373 (1961).

    CAS  Google Scholar 

  286. Lucas, F., J. T. B. Shaw and S. G. Smith: The Amino Acid Sequence in a Fraction of the Fibroin of Bombyx mori. Biochem. J. 66, 468 (1957).

    CAS  Google Scholar 

  287. Lukens, L. N.: Evidence for the Nature of the Precursor That is Hydroxy-lated during the Biosynthesis of Collagen Hydroxyproline. J. Biol. Chem. 240, 1661 (1965).

    CAS  Google Scholar 

  288. McEwen, M. B., M. I. Pratt and J. Randall: Scattering of Light by Collagen Solutions. In: Nature and Structure of Collagen, p. 158. London: Butter-worth Sei. Publ. 1953.

    Google Scholar 

  289. Malt, R. A. and P. T. Speakman: Ribosomal Aggregates Associated’with the Production of Collagen. Life Science 3, 81 (1964).

    CAS  Google Scholar 

  290. Manahan, J. and I. Mandl: Peptides Isolated from Collagenase-Collagen Digests. Biochem. Biophys. Res. Comm. 4, 368 (1961).

    CAS  Google Scholar 

  291. Mandelkern, L. and W. E. Stewart: The Effect of Neutral Salts on the Melting Temperature and Regeneration Kinetics of the Ordered Collagen Structure. Biochemistry 3, 1135 (1964).

    CAS  Google Scholar 

  292. Mandl, I.: Privatmitteilung.

    Google Scholar 

  293. Mandl, I.: Collagenases and Elastases. Adv. Enzymology 23, 163 (1961).

    CAS  Google Scholar 

  294. Mandl, I., L. T. Ferguson and S. F. Zaffuto: Exopeptidases of Clostridium histolyticum. Arch. Biochem. Biophys. 69, 565 (1957).

    CAS  Google Scholar 

  295. Mandl, I., S. Keller and B. Cohen: Microbial Elastases. A Comparative Study. Proc. Soc. Exp. Biol. Med. 109, 923 (1962).

    CAS  Google Scholar 

  296. Manner, G. and B. S. Gould: Collagen Biosynthesis. The Formation of Hydroxyproline and Soluble-Ribonucleic Acid Complexes of Proline and Hydroxyproline by Chick Embryo in vivo and by a Subcellular Chick Embryo System. Biochim. Biophys. Acta 72, 243 (1963).

    CAS  Google Scholar 

  297. Manner, G., B. S. Gould, A. Lebi and A. Schantz: Collagen Biosynthesis. Formation of an sRNA-Hydroxylysine Complex. 47th Annu. Meeting Federat. Amer. Soc. Exp. Biol., Atlantic City 1963, Abstr. 411.

    Google Scholar 

  298. Margoliash, E.: Primary Structure and Evolution of Cytochrome c. Proc. Nat. Acad. Sei. (USA) 50, 672 (1963).

    CAS  Google Scholar 

  299. Martin, G. R. and K. A. Piez: Biosynthesis and Maturation of Elastin. Collagen Symp. Somerville, N. J.: Ethicon, Inc., 1965.

    Google Scholar 

  300. Martin, G. R., K. A. Piez and M. S. Lewis: The Incorporation of [14C]-Glycine into the Subunits of Collagens from Normal and Lathyritic Animals. Biochim. Biophys. Acta 69, 472 (1963).

    CAS  Google Scholar 

  301. Maser, M. D. and R. V. Rice: Biophysical and Biochemical Properties of Earthworm-Cuticle Collagen. Biochim. Biophys. Acta 63, 255 (1962).

    CAS  Google Scholar 

  302. Maser, M. D. and R. V. Rice: Soluble Earthworm Cuticle Collagen: A Possible Dimer of Tropo-collagen. J. Cell Biol. 18, 569 (1963).

    CAS  Google Scholar 

  303. Mechanic, G. L. and M. Levy: An e-Lysine Tripeptide Obtained from Collagen. J. Amer. Chem. Soc. 81, 1889 (1959).

    CAS  Google Scholar 

  304. Mehl, J. W., J. L. Oncley and R. Simha: Viscosity and the Shape of Protein Molecules. Science 92, 132 (1940).

    CAS  Google Scholar 

  305. Meyer, A. und F. Verzär: Altersveränderung der Hydroxyprolin-Abgabe bei der thermischen Kontraktion von Kollagenfasern. Gerontologia 3, 184 (1959).

    CAS  Google Scholar 

  306. Meyer, K., E. Davidson, A. Linker and P. Hoffman: The Acid Mucopolysaccharides of Connective Tissue. Biochim. Biophys. Acta 21, 506 (1956).

    CAS  Google Scholar 

  307. Meyer, K., M. M. Grumbach, A. Linker and P. Hoffman: Excretion of Sulfated Mucopolysaccharides in Gargoylism (Hurler’s Syndrom). Proc. Soc. Exp. Biol. Med. 97, 275 (1958).

    CAS  Google Scholar 

  308. Michaels, S., P. M. Gallop, S. Seifter and E. Meilman: Studies on the Specificity of Collagenase. Biochim. Biophys. Acta 29, 451 (1958).

    Google Scholar 

  309. Millionova, M. I. and N. S. Andreeva: A Model of the Chain Configuration in Poly-(glycyl-L-proline). Biophysics (Biofizika) 3, 250 (1958).

    Google Scholar 

  310. Millionova, M. I. and N. S. Andreeva: On the Structure of Molecular Chain of Collagen. — The Structure of a Glycyl-L-proline Polymer. Biophysics (Biofizika) 2, 294 (1957); 4, No 3, 138 (1959).

    CAS  Google Scholar 

  311. Mitoma, C., T. E. Smith, F. Friedberg and C. R. Rayford: Incorporation of Hydroxyproline into Tissue Proteins by Chick-Embryos. J. Biol. Chem. 234, 78 (1959).

    CAS  Google Scholar 

  312. Morrione, T. G. and S. Seifter: Alteration in the Collagen Content of the Human Uterus during Pregnancy and Post Partum Involution. J. Exp. Medicine 115, 357 (1962).

    CAS  Google Scholar 

  313. Moss, J. A.: The Carbohydrate of Collagen. Biochem. J. 61, 151 (1955).

    Google Scholar 

  314. Muir, H.: Chemistry and Metabolism of Connective Tissue Glycosaminglycans (MPS). Intern. Rev. Conn. Tiss. Res. 2, 101 (1964).

    CAS  Google Scholar 

  315. Müller, W.: Die Serologie der chronischen Polyarthritis. Berlin: Springer- Verlag. 1962.

    Google Scholar 

  316. Nagai, Y.: Collagenase Digestion of Collagen. J. Biochemistry (Tokyo) 50, 486 (1961).

    CAS  Google Scholar 

  317. Nagai, Y. and H. Nöda: The Specificity of Collagenase. Biochim. Biophys. Acta 34, 298 (1959).

    CAS  Google Scholar 

  318. Nagai, Y., S. Sakakibara, H. Nöda and S. Akabori: Hydrolysis of Synthetic Peptides by Collagenase. Biochim. Biophys. Acta 37, 567 (1960).

    CAS  Google Scholar 

  319. Nagai, Y., S. Yagisawa and H. Nöda: Hydrolysis of Peptides Containing Sarcosine and Alanine by Collagenase. J. Biochemistry (Tokyo) 51, 382 (1962).

    CAS  Google Scholar 

  320. Nagamani, M. R.: Darstellung und Isolierung von Untereinheiten des Kollagens nach milder Hitzedenaturierung und alkalischer Behandlung. Diplomarbeit, Univ. München, 1963; Diss. 1965.

    Google Scholar 

  321. Nageotte, J.: Coagulation fibrillaire in vitro du collagène dissous dans un acide dilué. C. R. hebd. séances Acad. Sei. 184, 115 (1927).

    CAS  Google Scholar 

  322. Nemetschek, Th., W. Grassmann und U. Hofmann: Über die hochunterteilte Querstreifung des Kollagens. Z. Naturforsch. 106, 61 (1955).

    Google Scholar 

  323. Neuberger, A., J. C. Perrone and H. G. B. Slack: The Relative Metabolie Inertia of Tendon Collagen in the Rat. Biochem. J. 49, 199 (1951).

    CAS  Google Scholar 

  324. Neuman, R. E. and M. A. Logan: The Determination of Collagen and Elastin in Tissues. J. Biol. Chem. 186, 549 (1950).

    CAS  Google Scholar 

  325. Neuman, R. E. and M. A. Logan: The Determination of Hydroxyproline. J. Biol. Chem. 184, 299 (1950).

    CAS  Google Scholar 

  326. Nishigai, M., Y. Nagai and H. Nöda: Partial Collagenase Digestion of the Fiber Structure of Collagen. J. Biochemistry (Tokyo) 48, 152 (1960).

    CAS  Google Scholar 

  327. Nishihara, T.: Solubilization of Insoluble Collagen Fibers and Reconstitution Thereof. U. S.-Patent 3,034, 852 (1962).

    Google Scholar 

  328. Nishihara, T. and T. Miyata: The Effects of Proteases on the Soluble and Insoluble Collagen and the Structure of the Insoluble Collagen Fiber. Collagen Sympos. 3, 66 (1962).

    Google Scholar 

  329. Nöda, H. and R. W. G Wykoff: The Electron Microscopy of Reprecipitated Collagen. Biochim. Biophys. Acta 7, 494 (1951).

    Google Scholar 

  330. Nordwig, A.: Kollagenase und ihre Wirkung. Leder 13, 10 (1962).

    CAS  Google Scholar 

  331. Nordwig, A., G. Beier und Y. P. Dick: Unveröffentlicht.

    Google Scholar 

  332. Nordwig, A. and Y. P. Dick: Cleavage with Cyanogen Bromide of Methionyl Bonds in Collagen. Biochim. Biophys. Acta 97, 179 (1965).

    CAS  Google Scholar 

  333. Nordwig, A., H. Hörmann, K. Kühn und W. Grassmann: Weitere Versuche zum Abbau des Kollagens durch Kollagenase. Aminosäuresequenzen des Kollagens, IV. Z. physiol. Chem. 325, 242 (1961).

    CAS  Google Scholar 

  334. Oakley, C. L. and N. G. Banerjee: Bacterial Elastases. J. Pathol. Bacteriol. 85, 489 (1963).

    CAS  Google Scholar 

  335. Ogle, J. D., R. B. Arlinghaus and M. A. Logan: Studies on Peptides Obtained from Enzymic Digests of Collagen with Evidence for the Presence of an Unidentified Compound in this Protein. Arch. Biochem. Biophys. 94, 85 (1961).

    CAS  Google Scholar 

  336. Ogle, J. D., R. B. Arlinghaus and M. A. Logan: 3-Hydroxyproline, a New Amino Acid of Collagen. J. Biol. Chem. 237, 3667 (1962).

    CAS  Google Scholar 

  337. Orekhovich, V. N. and V. O. Shpikiter: Physicochemical Nature of Procollagen. In: G. Stainsby (Edit.), Recent Advances in Gelatin and Glue Research, p. 87. London: Pergamon Press. 1958.

    Google Scholar 

  338. Orekhovich, V. N. and V. O. Shpikiter: Procollagens. Science 127, 137 (1958).

    Google Scholar 

  339. Orekhovich, V. N., V. O. Shpikiter, V. I. Mazourovet, O. V. Kounina: Procollagènes. Classification, métabolisme, action des protéinases. Bull. soc. chim. biol. (Paris) 42, 505 (1960).

    CAS  Google Scholar 

  340. Orekhovich, V. N., A. A. Tustanovski, K. D. Orekhovich and N. E. Plotnikova: Procollagen of Hide. Biokhimiya (USSR) 13, 55 (1948).

    CAS  Google Scholar 

  341. Orekhovich, V. N., A. A. Tustanovski and N. E. Plotnikova: C. R. (Doklady) Acad. Sei. (USSR) 60, 837 (1954).

    Google Scholar 

  342. Partridge, S. M.: The Constitution and Biosynthesis of the Cross Linkages in Elastin. Symp. Internat. Biochim. Physiol. Tissu Conjonctif. Lyon, 1965.

    Google Scholar 

  343. Pauling, L. and R. B. Corey: The Pleated Sheet, a new Layer Configuration of Polypeptide Chains. Proc. Nat. Acad. Sei. (USA) 37, 251 (1951).

    CAS  Google Scholar 

  344. Pauling, L. and R. B. Corey: The Structure of Fibrous Proteins of the Collagen-Gelatin Group. Proc. Nat. Acad. Sei. (USA) 37, 272 (1951).

    CAS  Google Scholar 

  345. Pauling, L., R. B. Corey and H. R. Branson: The Structure of Proteins: Hydrogen-bonded Helical Configurations of the Polypeptide Chain. Proc. Nat. Acad. Sei. (USA) 37, 205 (1951).

    CAS  Google Scholar 

  346. Peterkofsky, B. and S. Udenfriend: Conversion of Proline to Collagen Hydroxyproline in a Cell-free System from Chick Embryo. J. Biol. Chem. 238, 3966 (1963).

    CAS  Google Scholar 

  347. Peterkofsky, B. and S. Udenfriend: Enzymatic Hydroxylation of Proline in Microsomal Polypeptide Leading to Formation of Collagen. Proc. Nat. Acad. Sei. (USA) 53, 335 (1965).

    CAS  Google Scholar 

  348. Peterlin, A.: Light Scattering and Small Angle X-Ray Scattering by Macro-molecular Coils with Finite Persistence Lenght. J. Polymer Sei. 47, 403 (1960).

    CAS  Google Scholar 

  349. Piez, K. A.: Nonidentity of the Three a-Chains in Codfish Skin Collagen. J. Biol. Chem. 239, PC 4315 (1964).

    Google Scholar 

  350. Piez, K. A. and A. L. Carrillo: Helix Formation by Single-and Double- Chain Gelatins from Rat Skin Collagen. Biochemistry 3, 908 (1964).

    CAS  Google Scholar 

  351. Piez, K. A., E. A. Eigner and M. S. Lewis: The Chromatographic Separation and Amino Acid Composition of the Subunits of Several Collagens. Biochemistry 2, 58 (1963).

    CAS  Google Scholar 

  352. Piez, K. A. and J. Gross: The Amino Acid Composition and Morphology of Some Invertebrate and Vertebrate Collagens. Biochim. Biophys. Acta 34, 24 (1959).

    CAS  Google Scholar 

  353. Piez, K. A., M. S. Lewis, G. R. Martin and J. Gross: Subunits of the Collagen Molecule. Biochim. Biophys. Acta 53, 596 (1961).

    CAS  Google Scholar 

  354. Petruska, J. A. and A. J. Hodge: A Subunit Model for the Tropocollagen Macromolecule. Proc. Nat. Acad. Sei. (USA) 51, 871 (1964).

    CAS  Google Scholar 

  355. Popenoe, E. A. and D. D. van Slyke: The Formation of Collagen Hydroxy-lysine. J. Biol. Chem. 237, 3491 (1962).

    CAS  Google Scholar 

  356. Prockop, D. J.: Synthesis of Collagen. Nature 194, 477 (1962).

    CAS  Google Scholar 

  357. Prockop, D. J., P. S. Ebert and B. M. Shapiro: Studies with Proline-3,4-H3 on the Hydroxylation of Proline during Collagen Synthesis in Chick Embryos. Arch. Biochem. Biophys. 106, 112 (1964).

    CAS  Google Scholar 

  358. Prockop, D. J. and K. Juva: Hydroxylation of Proline in Particulate Fractions from Cartilage. Biochem. Biophys. Res. Comm. 18, 54 (1965).

    CAS  Google Scholar 

  359. Prockop, D. J. and K. Juva: Synthesis of Hydroxyproline in vitro by the Hydroxylation of Proline in a Precursor of Collagen. Proc. Nat. Acad. Sei. (USA) 53, 661 (1965).

    CAS  Google Scholar 

  360. Prockop, D. (J.), A. Kaplan and S. Udenfriend: Oxygen-18 Studies on the Conversion of Proline to Collagen Hydroxyproline. Arch. Biochem. Biophys. 101, 499 (1963).

    CAS  Google Scholar 

  361. Prockop, D. J., B. Peterkofsky and S. Udenfriend: Studies on the Intracellular Localization of Collagen Synthesis in the Intact Chick Embryo. J. Biol. Chem. 237, 1581 (1962).

    CAS  Google Scholar 

  362. Prockop, D. J., O. Pettengill and H. Holtzer: Incorporation of Sulfate and the Synthesis of Collagen by Cultures of Embryonic Chondrocytes. Biochim. Biophys. Acta 83, 189 (1964).

    CAS  Google Scholar 

  363. Prockop, D. J. and S. Udenfriend: A Specific Method for the Analysis of Hydroxyproline in Tissues and Urine. Analyt. Biochem. 1, 228 (1960).

    CAS  Google Scholar 

  364. Ramachandran, G. N.: Structure of Collagen. Nature 177, 710 (1956).

    CAS  Google Scholar 

  365. Ramachandran, G. N. and G. Kartha: Structure of Collagen. Nature 174, 269 (1954).

    CAS  Google Scholar 

  366. Ramachandran, G. N. and G. Kartha: Structure of Collagen. Nature 176, 593 (1955).

    CAS  Google Scholar 

  367. Ramachandran, G. N. and V. Sasisekharan: Structure of Collagen. Nature 190, 1004 (1961).

    CAS  Google Scholar 

  368. Ramachandran, G. N., V. Sasisekharan and Y. T. Thathachari: Structure of Collagen at the Molecular Level. In: N. Ramanathan (Edit.), Collagen, p. 81. London: Interscience Publ. 1962.

    Google Scholar 

  369. Randall, J. T.: Observations on the Collagen System. J. Soc. Leather Trades ’ Chem. 38, 362 (1954).

    CAS  Google Scholar 

  370. Randall, J. T., R. D. B. Fräser, S. F. Jackson, A. V. M. Martin and A. C. T. North: Aspects of Collagen Structure. Nature 169, 1029 (1952).

    CAS  Google Scholar 

  371. Randall, J. T., R. D. B. Fraser and A. C. T. North: The Structure of Collagen. Proc. Roy. Soc. (London) B 141, 62 (1953).

    CAS  Google Scholar 

  372. Rice, R. Y.: Reappearance of Certain Structural Features of Native Collagen after Thermal Transformation. Proc. Nat. Acad. Sei. (USA) 46, 1186 (1960).

    CAS  Google Scholar 

  373. Rice, R. V., E. F. Casassa, R. E. Kerwin and M. D. Maser: On the Length and Molecular Weight of Tropocollagen from Calf Skin. Arch. Biochem. Bio-phys. 105, 409 (1964).

    CAS  Google Scholar 

  374. Rich, A. and F. H. C. Crick: The Structure of Collagen. Nature 176, 915 (1955).

    CAS  Google Scholar 

  375. Rich, A. and F. H. C. Crick: The Structure of Collagen. In: G. Stainsby (Edit.), Recent Advances in Gelatin and Glue Research, p. 20. London: Pergamon Press. 1958.

    Google Scholar 

  376. Rich, A. and F. H. C. Crick: The Molecular Structure of Collagen. J. Mol. Biol. 3, 483 (1961).

    CAS  Google Scholar 

  377. Rigby, B. J.: Thermal Transitions in Normal and Deuterated Rat Tail Tendon, Human Skin, and Tuna-fish Skin. Biochim. Biophys. Acta 62, 183 (1962).

    CAS  Google Scholar 

  378. Robertson, W. van B.: The Biochemical Role of Ascorbic Acid in Connective Tissue. Ann. New York Acad. Sei. 92, 159 (1961).

    CAS  Google Scholar 

  379. Robertson, W. van B.: D-Ascorbic Acid and Collagen Synthesis. Biochim. Biophys. Acta 74, 137 (1963).

    CAS  Google Scholar 

  380. Robertson, W. van B. and B. Schwartz: Ascorbic Acid and the Formation of Collagen. J. Biol. Chem. 201, 689 (1953).

    Google Scholar 

  381. Rogulenkova, V. N., M. I. Millionova and N. S. Andreeva: On the Close Structural Similarity between poly-Gly-L-Pro-L-Hypro and Collagen. J. Mol. Biol. 9, 253 (1964).

    CAS  Google Scholar 

  382. Romeis, B.: Mikroskopische Technik, S. 167. München: Leibnitz Verl. 1948.

    Google Scholar 

  383. Ross, R. and E. P. Benditt: A Comparison of the Utilization of Proline-H3 in Healing Wounds as Seen by Electron Microscope-Autoradiography. 47 th Annu. Meeting Federat. Amer. Soc. Exp. Biol., Atlantic City, 1963, Abstr. No. 178.

    Google Scholar 

  384. Ross, R. and E. P. Benditt: Altered Configuration of Ribosomes in Scorbutic Fibroblasts. Federat. Proc. (Amer. Soc. Exp. Biol.) 23, 441 (1964).

    Google Scholar 

  385. Rubin, A. L., D. Pfahl, P. T. Speakman, P. F. Davison and F. O. Schmitt: Tropocollagen: Significance of Protease-Induced Alterations. Science 139, 37 (1963).

    CAS  Google Scholar 

  386. Sanger, F.: The Terminal Peptides of Insulin. Biochem. J. 45, 563 (1949).

    CAS  Google Scholar 

  387. Scharpensel, H. W. und G. Wolf: In vitro-Kollagen-Synthese in foetalen Hautpräparaten. Z. Tierphysiol. Tierernähr. Futtermittelk. 14, 347 (1959).

    Google Scholar 

  388. Schaub, M. C.: Degradation of Young and Old Collagen by Extracts of Various Organs. Gerontologia 9, 52 (1964).

    Google Scholar 

  389. Schaub, M. C.: A Collagen Degrading Mechanism in the Rat Uterus During Post-Partum Involution. Helv. Physiol. Pharm. Acta 21, 227 (1963).

    CAS  Google Scholar 

  390. Scheraga, H. A. and L. Mandelkern: Consideration of the Hydrodynamic Properties of Proteins. J. Amer. Chem. Soc. 75, 179 (1953).

    CAS  Google Scholar 

  391. Scherrer, P.: Zsigmondys Lehrbuch der Kolloidchemie, 3. Auflage, S. 408. Leipzig: O. Spanner. 1920.

    Google Scholar 

  392. Schleyer, M.: Trennung der α- und β-Komponenten aus Tropokollagen. Aminosäuresequenzen des Kollagens, V. Z. physiol. Chem. 329, 97 (1962).

    CAS  Google Scholar 

  393. Schmitt, F. O.: Macromolecular Interaction Patterns in Biological Systems. Proc. Amer. Philos. Soc. 100, 476 (1956).

    CAS  Google Scholar 

  394. Schmitt, F. O.: Ultrastructure and the Problem of Cellular Organization. Harvey Lect. 40, 249 (1944–45).

    CAS  Google Scholar 

  395. Schmitt, F. O. and J. Gross: Further Progress in the Electron Microscopy of Collagen. J. Amer. Leather Chem. Assoc. 43, 658 (1948).

    CAS  Google Scholar 

  396. Schmitt, F. O., J. Gross and J. H. Highberger: A New Particle Type in Certain Connective Tissue Extracts. Proc. Nat. Acad. Sei. (USA) 39, 459 (1953).

    CAS  Google Scholar 

  397. Schmitt, F. O., J. Gross and J. H. Highberger: States of Aggregation of Collagen. Sympos. Soc. Exp. Biol. 9, 148 (1955).

    Google Scholar 

  398. Schmitt, F. O., C. E. Hall and M. A. Jakus: Electron Microscope Investigations of the Structure of Collagen. J. Cell. Comp. Physiol. 20, 11 (1942).

    CAS  Google Scholar 

  399. Schmitt, F. O., C. E. Hall and M. A. Jakus: Fine Structure in the Fiber-Axis Macroperiod of Collagen Fibrils. J. Appl. Phys. 16, 263 (1945).

    Google Scholar 

  400. Schneider, W. und Hj. Staudinger: Zum Wirkungsmechanismus von Vitamin C. Klin. Wschr. 42, 879 (1964).

    CAS  Google Scholar 

  401. Schroeder, W. A., L. Honnen and F. C. Green: Chromatographic Separation and Identification of Some Peptides in Partial Hydrolysates of Gelatin. Proc. Nat. Acad. Sei. (USA) 39, 23 (1953).

    CAS  Google Scholar 

  402. Schroeder, W. A., L. M. Kay, J. LeGette, L. Honnen and F. C. Green: The Constitution of Gelatin. Separation and Estimation of Peptides in Partial Hydrolysates. J. Amer. Chem. Soc. 76, 3556 (1954).

    CAS  Google Scholar 

  403. Schrohenloher, R. E., J. D. Ogle and M. A. Logan: Two Tripeptides from an Enzymatic Digest of Collagen. J. Biol. Chem. 234, 58 (1959).

    CAS  Google Scholar 

  404. Schwarz, W. und H. J. Merker: Die Fibrillogenese in verschiedenen Binde-gewebsformen des menschlichen Embryos. Beitr. Silikose-Forsch., Sonder-band 4, 231 (1960).

    CAS  Google Scholar 

  405. Seifter, S., P. M. Gallop and C. Franzblau: Some Aspects of Collagenolytic Action. Trans. New York Acad. Sei. 23, 540 (1961).

    CAS  Google Scholar 

  406. Seifter, S., P. M. Gallop, L. Klein and E. Meilman: Studies on Collagen. II. Properties of Purified Collagenase and its Inhibition. J. Biol. Chem. 234, 285 (1959).

    CAS  Google Scholar 

  407. Sheldon, H. and F. B. Kimball: Studies on Cartilage. III. The Occurrence of Collagen within Vacuoles of the Golgi Apparatus. J. Cell Biol. 12, 599 (1962).

    CAS  Google Scholar 

  408. Shintani, Y. K. and H. E. Taylor: Radioautographic Study of S3504 Uptake by Epiphyseal Cartilage in Experimental Lathyrism. Cañad. J. Biochem. Physiol. 40, 565 (1962).

    CAS  Google Scholar 

  409. Sinex, F. M., D. D. van Slyke and D. R. Christman: The Source and State of the Hydroxylysine of Collagen. J. Biol. Chem. 234, 918 (1959).

    CAS  Google Scholar 

  410. Siuko, H., J. Sävelä and E. Kulonen: Effect of the Hydrocortisone on the Formation of Collagen in Guinea Pig Skin. Acta Endocrinol. 31, 113 (1959).

    CAS  Google Scholar 

  411. Smiley, J. D., H. Yeager and M. Ziff: Collagen Metabolism in Osteolathyrism in Chick Embryos: Site of Action of ß-Aminopropionitrile. J. Exp. Medicine 116, 45 (1962).

    CAS  Google Scholar 

  412. Smith, D. J. and R. C. Shuster: Biochemistry of Lathyrism. I. Collagen Biosynthesis in Normal and Lathyritic Chick Embryos. Arch. Biochem. Biophys. 98, 498 (1962)

    CAS  Google Scholar 

  413. Smith, E. L.: Dipeptidases. In: S. P. Colowick and N. O. Kaplan (Edit.). Methods in Enzymology, Vol. II, p. 93. New York: Academic Press. 1955.

    Google Scholar 

  414. Snellman, O.: A Glycoprotein from Reticulin Tissue. —: Studies on a Matrix for the Biosynthesis of Collagen. — Biosynthesis of Collagen Performed in vitro with the Aid of a Matrix Occurring in Reticulin. Acta Chem. Scand. 17, 1049, 1057, 1062 (1963).

    Google Scholar 

  415. Sobel, A. E.: Multiple Mechanism of Nucleation. Proc., 2nd Europ. Sympos. on Calcified Tissues, Lüttich 1964.

    Google Scholar 

  416. Solomons, C. C. and J. T. Irving: The Reaction of some Hard-and Soft- Tissue Collagens with i-Fluoro-2,4-Dinitrobenzene. Biochem. J. 68, 499 (1958).

    Google Scholar 

  417. Stacy, K. A.: Light Scattering in Physical Chemistry. London: Butterworth Sei. Publ. 1956.

    Google Scholar 

  418. Stadler, P. und W. Träsch: Fluoreszenzfärbungen an tierischem Hautmaterial. Leder 10, 213 (1959).

    CAS  Google Scholar 

  419. Stegemann, H.: Mikrobestimmung von Hydroxyprolin mit Chloramin T und p-Dimethylaminobenzaldehyd. Z. physiol. Chem. 311, 41 (1958).

    CAS  Google Scholar 

  420. Stetten, M. R.: Some Aspects of the Metabolism of Hydroxyproline, Studied with the Aid of Isotopic Nitrogen. J. Biol. Chem. 181, 31 (1949).

    CAS  Google Scholar 

  421. Steven, F. S. and G. R. Tristram: The Origin of N-Terminal Residues in Acetic Acid-Soluble Calf-Skin Collagen. Biochem. J. 83, 245 (1962).

    Google Scholar 

  422. Strauch, L. und W. Grassmann: Reinigung von Kollagenase, III. Gewinnung enzymatisch einheitlicher Kollagenase. Z. physiol. Chem. (im Druck).

    Google Scholar 

  423. Takahushi, T. and W. Yokoyama: Physico-Chemical Studies on the Skin and Leather of Marine Animals. 12. The Content of Hydroxyproline in the Collagen of Different Fish Skins. Bull. Jap. Soc. Scient. Fisheries 20, 525 (1954).

    Google Scholar 

  424. Taylor, E. W. and W. Cramer: Birefringence of Protein Solutions, and Biological Systems. I.; II. Studies on TMV, Tropocollagen, and Paramyosin. Biophys. J. 3, 128, 143 (1963).

    CAS  Google Scholar 

  425. Thomas, J., D. F. Elsden and S. M. Partridge: Partial Structure of Two Major Degradation Products from the Cross-linkages in Elastin. Nature 200, 651 (1963).

    CAS  Google Scholar 

  426. Tristram, G. R.: The Amino Acid Composition of Proteins. In: H. Neurath and K. Bailey (Edit.), The Proteins, Vol.1, Part A, p. 181. New York: Academic Press. 1953.

    Google Scholar 

  427. Tromans, W. J., R. W. Horne, G. A. Gresham and A. J. Bailey: Electron Microscope Studies on the Structure of Collagen Fibrils by Negative Staining. Z. Zellforsch. 58, 798 (1963).

    CAS  Google Scholar 

  428. Urivetzky, M., J. M. Frei and E. Meilman: Cell-Free Collagen Biosynthesis and the Hydroxylation of sRNA-Proline. Arch. Biochem. Biophys. 109, 480 (1965).

    CAS  Google Scholar 

  429. Veis, A., J. Anesey and J. Cohen: The Long Range Reorganization of Gelatin to the Collagen Structure. Arch. Biochem. Biophys. 94, 20 (1961).

    CAS  Google Scholar 

  430. Verzär, F.: Veränderungen der thermoelastischen Kontraktion von Sehnenfasern im Alter. Helv. Physiol. Pharmacol. Acta 13, C 64 (1955).

    Google Scholar 

  431. Verzär, F.: Das Altern des Kollagens. Helv. Physiol. Pharmacol. Acta 14, 207 (1956).

    Google Scholar 

  432. Verzär, F.: Nachweis der Zunahme der Bindung von Hydroxyprolinen im Kollagen der Haut mit dem Alter. Gerontologia 4, 105 (1960).

    Google Scholar 

  433. Verzär, F.: Aging of the Collagen Fiber. In: D. A. Hall (Edit.), International Revue of Conn. Tiss. Res. Vol. II, p. 243. New York: Academic Press. 1964. Vgl. dazu Übersicht von Verzär.

    Google Scholar 

  434. Verzär, F.: Differenzierung verschiedener Vernetzungen (Crosslinks) des Kollagens durch Spannungsmessungen. Z. physiol. Chem. 335, 38 (1963).

    Google Scholar 

  435. Verzär, F. and K. Huber: Thermic-Contraction of Single Tendon Fibres from Animals of Different Age after Treatment with Formaldehyde, Urethane, Glycerol, Acetic Acid and Other Substances. Gerontologia 2, 81 (1958).

    Google Scholar 

  436. Vogel, G. und L. Ther: Untersuchungen über den Einfluß endokriner Faktoren auf die Reißfestigkeit bindegewebiger Strukturen. Naunyn Schmiedeberg’s Arch. exp. Pathol. Pharmakol. 246, 72 (1963).

    Google Scholar 

  437. Waldschmidt-Leitz, E. und O. Zeiss: Über Protofibroin, die kristalline Hauptkomponente der Seidenfaser. Z. physiol. Chem. 300, 49 (1955).

    CAS  Google Scholar 

  438. Walsh, K. A., D. L. Kauffman, K. S. V. Sampath Kumar and H. Neurath: On the Structure and Function of Bovine Trypsinogen and Trypsin. Proc. Nat. Acad. Sei. (USA) 51, 301 (1964).

    CAS  Google Scholar 

  439. Watson, J. D.: Die Beteiligung der Ribonucleinsäure an der Proteinsynthese. Angew. Chem. 75, 439 (1963).

    CAS  Google Scholar 

  440. Watson, M. R.: The Chemical Composition of Earthworm Cuticle. Biochem. J. 68, 416 (1958).

    CAS  Google Scholar 

  441. Watson, M. R. and N. R. Silvester: Studies of Invertebrate Collagen Preparations. Biochem. J. 71, 578 (1959).

    CAS  Google Scholar 

  442. Weigert, C.: Über eine Methode zur Färbung elastischer Fasern. Zbl. Pathol. 9, 289 (1898).

    Google Scholar 

  443. Wiederhorn, N. M. and G. V. Reardon: Studies Concerned with the Structure of Collagen. II. Stress-Strain Behavior of Thermally Contracted Collagen. J. Polymer Sei. 9, 315 (1952).

    CAS  Google Scholar 

  444. Williams, A. P.: The Chemical Composition of Snail Gelatin. Biochem. J. 74, 304 (1960).

    CAS  Google Scholar 

  445. Wilm, M. v.: Chemische Veränderungen an den funktionellen Gruppen des Kollagens. Dissert., Univ. München, 1965.

    Google Scholar 

  446. Woessner, J. F., Jr.: Catabolism of Collagen and Non-collagen Protein in the Rat Uterus during Post-partum Involution. Biochem. J. 83, 304 (1962).

    CAS  Google Scholar 

  447. Woessner, J. F., Jr.: The Determination of Hydroxyproline in Tissue and Protein Samples Containing Small Proportions of this Imino Acid. Arch. Biochem. Biophys. 93, 440 (1961).

    CAS  Google Scholar 

  448. Woessner, J. F., Jr. and T. H. Brewer: Formation and Breakdown of Collagen and Elastin in the Human Uterus during Pregnancy and Post-Partum Involution. Biochem. J. 89, 75 (1963).

    CAS  Google Scholar 

  449. Wolf, G., and C. R. A. Berger: The Metabolism of Hydroxyproline in the Intact Rat. Incorporation of Hydroxyproline into Protein and Urinary Metabolites. J. Biol. Chem. 230, 231 (1958).

    CAS  Google Scholar 

  450. Wolpers, C.: Kollagenquerstreifung und Grundsubstanz. Klin. Wschr. 22, 624 (1943).

    Google Scholar 

  451. Wolpers, C.: Zur elektronenmikroskopischen Darstellung elastischer Gewebselemente. Klin. Wschr. 23, 169 (1944).

    Google Scholar 

  452. Wolpers, C.: Das Scheiben-und das Lamellenstadium der Kollagenquerstreifung. Makromolek. Chem. 2, 37 (1948).

    CAS  Google Scholar 

  453. Wolpers, C.: Kollagenquerstreifung und Hitzeschrumpfung. Biochem. Z. 318, 373 (1948).

    CAS  Google Scholar 

  454. Wood, G. C.: 4th Internat. Congr. Biochem., Vienna, 1958, Abstr. No. 2–92, p. 26.

    Google Scholar 

  455. Wood, G. C.: The Formation of Fibrils from Collagen Solutions. 2. A Mechanism of Collagen-Fibril Formation. Biochem. J. 75, 598 (1960).

    CAS  Google Scholar 

  456. Wood, G. C.: The Formation of Fibrils from Collagen Solutions. 3. Effect of Chon-droitin Sulphate and Some other Naturally Occuring Polyanions on the Rate of Formation. Biochem. J. 75, 605 (1960).

    CAS  Google Scholar 

  457. Wood, G. C.: The Heterogeneity of Collagen Solutions. Biochem. J. 82, 2p (1962).

    Google Scholar 

  458. Wood, G. C.: The Heterogeneity of Collagen Solutions and its Effect on Fibril Formation. Biochem. J. 84, 429 (1962).

    CAS  Google Scholar 

  459. Wood, G. C. and M. K. Keech: The Formation of Fibrils from Collagen Solutions. 1. The Effect of Experimental Conditions: Kinetic and Electron-Microscope Studies. Biochem. J. 75, 588 (1960).

    CAS  Google Scholar 

  460. Wünsch, E. und H. G. Heidrich: Darstellung von Prolinpeptiden, III. Ein neues Substrat zur Bestimmung der Kollagenase. Z. physiol. Chem. 332, 300 (1963).

    Google Scholar 

  461. Wuthier, R. E., P. Gron and J. T. Irving: The Reaction of i-Fluoro-2,4- dinitrobenzene with Bone. Studies on the Relationship between Bone Collagen and Apatite. Biochem. J. 92, 205 (1964).

    CAS  Google Scholar 

  462. Yamazaki, I., H. S. Mason and L. (H.) Piette: Identification by Electron Paramagnetic Resonance Spectroscopy, of Free Radicals Generated from Substrates by Peroxidase. J. Biol. Chem. 235, 2444 (1960).

    CAS  Google Scholar 

  463. Yamazaki, I. and L. H. Piette: Mechanism of Free Radical Formation and Disappearance during the Ascorbic Acid Oxidase and Peroxidase Reactions. Biochim. Biophys. Acta 50, 62 (1961).

    CAS  Google Scholar 

  464. Yip, C. C.: The Hydroxylation of Proline by Horseradish Peroxidase. Biochim. Biophys. Acta 92, 395 (1964).

    CAS  Google Scholar 

  465. Yonath, J., A. Oplatka and A. Katchalsky: Equilibrium Mechanochemistry of Collagen Fibers. Conference on the Structure and Function of Connective and Skeletal Tissues. St. Andrews (Scotland), 1964.

    Google Scholar 

  466. Young, E. G. and J. W. Lorimer: A Comparison of the Acid-Soluble Collagens from the Skin and Swim Bladder of the Cod. Arch. Biochem. Biophys. 92, 183 (1961).

    CAS  Google Scholar 

  467. Yphantis, D. A.: Rapid Determination of Molecular Weights of Peptides and Proteins. Ann. New York Acad. Sei. 88, 586 (1960).

    CAS  Google Scholar 

  468. Zimm, B. H. and J. K. Bragg: Theory of Phase Transition between Helix and Random Coil in Polypeptide Chains. J. Chem. Phys. 31, 526 (1959).

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. München, Deutschland

    W. Grassmann, J. Engel, K. Hannig, H. Hörmann, K. Kühn & A. Nordwig

Authors
  1. W. Grassmann
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. J. Engel
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. K. Hannig
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. H. Hörmann
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. K. Kühn
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. A. Nordwig
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. California Institute of Technology, Pasadena, USA

    L. Zechmeister

Rights and permissions

Reprints and permissions

Copyright information

© 1965 Springer-Verlag/Wien

About this chapter

Cite this chapter

Grassmann, W., Engel, J., Hannig, K., Hörmann, H., Kühn, K., Nordwig, A. (1965). Kollagen.(Collagen.). In: Zechmeister, L. (eds) Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrès dans la Chimie des Substances Organiques Naturelles. Fortschritte der Chemie organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products, vol 23. Springer, Vienna. https://doi.org/10.1007/978-3-7091-7139-4_5

Download citation

  • DOI: https://doi.org/10.1007/978-3-7091-7139-4_5

  • Publisher Name: Springer, Vienna

  • Print ISBN: 978-3-7091-7141-7

  • Online ISBN: 978-3-7091-7139-4

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation