Abstract
It has been the hope of the biochemist for more than half a century to study in vitro the biological, i. e. enzymatic synthesis of protein. Of course, the hope has not yet been realized; but the outlook is brighter, or at least, less dim now. Certain misconceptions have been recognized, and with the removal of these obstructions approaches to the core of the problem appear to have been opened. This advance was made possible by the new experimental tool of isotope-labeled tracers. In most in vitro chemical reactions the products are formed in large enough quantities to be measured. This is not the case in protein biosynthesis, first because the reaction is very slow compared with ordinary chemical reactions, and second because a relatively large amount of protein is needed as enzyme system to make the reaction go at all; and any small increase in protein that may occur has to be seen against the backgroand of the large amount of protein present initially. The latter difficulty is now being circumvented, to some extent, by the use of antibodies to precipitate small amounts of specific proteins formed, [Petters and Anfinsen (129, 130), Keston and Dreyfus (100)]. But even in these experiments it is possible that there has not been an increase in the mass of total protein, but only a transformation of one tissue protein into another.
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References
Abdou, I. A. and H. Tarver: Plasma Protein. II. Relationship between Circulating and Tissue Protein. J. biol. Chemistry 190, 781 (1951).
Abrams, R., J. M. Goldingerand E. S. G. Barron: Synthesis of Protein and Other Cell Substances from Acetic Acid in Isolated Bone Marrow. Biochim. Biophys. Acta 5, 74 (1950)
Anfinsen, C. B.: Radioactive Crystalline Ribonuclease. J. biol. Chemistry 185, 827 (1950).
Anfinsen, C. B.: The Nature of Intermediates in Protein Synthesis. Science (New York) 114, 683 (1951).
Anfinsen, C: B., A. B.loff, A. B. Hastingsand A. K. Solomon: The In Vitra Turnover of Dicarboxylic Amino Acids in Liver Slice Proteins. J. biol. Chemistry 168, 771 (1947)
Anfinsen, C. B. and D. Steinberg: Studies on the Biosynthesis of Ovalbumin. J. biol. Chemistry 189, 739 (1951)
Angier, R. B., J. H. Boothe, B. L. Hutchings, J. H. Mowat. J. Semb, E. L. R. Stokstad, Y. Subbarow, C. W. Waller, D. B. Consijeich, M. J. Fahrenbach, M. E. Hultquist, E. Kuh, E. H. Northey, D. R. Seeger, J. P. Sickels and J. M. Smith, Jr.: The Structure and Synthesis of the Liver L. Casei Factor. Science (New York) 103, 667 (1946).
Barker, H. A.: Recent Investigations on the Formation and Utilization of Active Acetate. In: W. D. Mcelroy and B. Glass, A Symposium on Phosphorus Metabolism, pp. 240–241. Baltimore: John Hopkins Press. 1951.
Bergmann, M. and O. K. Behrens: On the Assymmetric Course of the Enzymatic Synthesis of Peptide Bonds. J. biol. Chemistry 124, 7 (1938).
Bergmann, M. and H. Fraenkel-Conrat: The Rôle of Specificity in the Enzymatic Synthesis of Proteins. Syntheses with Intracellular Enzymes. J. biol. Chemistry 119, 707 (1937).
Bergmann, M. and H. Fraenkel-Conrat: The Enzymatic Synthesis of Peptide Bonds. J. biol. Chemistry 124, 1 (1938).
Bergmann, M. and J. S. Fruton: Some Synthetic and Hydrolytic Experiments with Chymotrypsin. J. biol. Chemistry 124, 321 (1938)
Bergmann, M. and J. S. Fruton: The Significance of Coupled Reactions for the Enzymatic Hydrolysis and Synthesis of Proteins. Ann. Yew York Acad. Sci. 45, 409 (1944).
Brocu, K.: A Heat Stable Co-factor for Glutathione Synthesis. Federat. Proc. (Amer. Soc. ezp. Biol.) 80, 163 (1951).
Bodansky, O.: Introduction to Physiological Chemistry, p. 280. New York: J. Wiley and Sons. 1938.
Borsook, H.: Protein Turnover and Incorporation of Labeled AminQ Acids into Tissue Proteins In Vivo and In Vitro. Physiologic. Rev. 30, 206 (1950).
Borsook, H.: (unpublished).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: The Incorporation of Labeled Lysine into the Proteins of Guinea Pig Liver Homogenate. J. biol. Chemistry 279, 689 (1949).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: A Peptide Fraction in Liver. J. biol. Chemistry 179, 705 (1949).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: Uptake of Labeled Amino Acids by Tissue Proteins In Vitro. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 589 (1949)
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: The Uptake In Vitro of Cm-Labeled Glycine, L-Leucine, and L-Lysine by Different Components of Guinea Pig Liver Homogenate. J. biol. Chemistry 184, 529 (1950).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: Metabolism of C14-Labeled Glycine, L-Histidine, L-Leucine and L-Lysine. J. biol. Chemistry 187, 839 (1950).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: Incorporation In Vitro of Labeled Amino Acids into Bone Marrow Cell Proteins. J. biol. Chemistry, 86, 297 (1950).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighleyand P. H. Lowy: Incorporation In Vitro of Labeled Amino Acids into Rat Diaphragm Proteins. J. biol. Chemistry 186, 309 (1950).
Borsook, H., C. L. Deasy, A. J Haagen-Smit, G. Keighley and P. H. Lowy: Incorporation In Vitro of Labeled Amino Acids into Proteins of Rabbit Reticulocytes. J. biol. Chemistry 196, 669 (1952).
Borsook, H. and J. W. Dubnoff: The Biological Synthesis of Hippuric Acid In Vitro. J. biol. Chemistry 132, 307 (1940).
Borsook, H. and J. W. Dubnoff: Synthesis of Hippuric Acid in Liver Homogenate. J. biol. Chemistry 268, 397 (1947)
Borsook, H. and J. W. Dubnoff: (unpublished).
Borsook, H. and H. M. Huffman: Some Thermodynamical Considerations of Amino Acids, Peptides, and Related Substances. In Claschmidt, Chemistry of the Amino Acids and Proteins, p. 822. Springfield, III. — Baltimore. 1938.
Borsook, H. and G. L. Keighley: The Continuing Metabolism of Nitrogen in Animals. Proc. Roy. Soc. (London), Ser. B 118, 488 (1935).
Brachet, J.: Recherches sur la synthèse de l’acide thymonucléique pendant le développement de l’oeuf d’oursin. Arch. Biol. (Paris) 44, 519 (1933)
Brachet, J.: The Metabolism of Nucleic Acid during Embryonic Development. Cold Spring Harbor Symp. Quant. Biology 12, 18 (1947).
Brenner, M., H. R. Millerand R. W. Pfister: Eine neue enzymatische Peptidsynthese. Helv. chim. Acta 33, 568 (1950).
Brenner, M. and R. W. Pfister: Enzymatische Peptidsynthese. Isolierung von enzymatisch gebildetem L-Methionyl-L-methionin and L-Methionyl-Lmethionyl-L-methionin Helv. shim. Acta 34, 2085 (1951).
Brenner, M., E. Sailerand K. Rüfenacht: Enzymatische Peptidsynthese. Peptidbildung aus DL-Threonin-isopropyl-ester. Helv. chim. Acta 34, 2096 (1951)
Cannon, P. R., C. H. Steffee, L. J. Frazier, D. A. Rowleyand P. C. Stepto: The Influence of Time of Ingestion of Essential Amino Acids upon Utilization in Tissue-Synthesis. Federat. Proc. (Amer. Soc. exp. Biol.) 6, 390 (1947)
Casperrson, T. and K. Brandt: Nucleotidumsatz and Wachstum bei PreB- hefe. Protoplasma 35, 507 (1940/41).
Casperrson, T., H. Landström-Hydan and L. Aquilonius: CytOplasmanukleotide in eiweißproduzierenden Drüsenzellen. Chromosome 2, 111 (1941–1944).
Casperrson, T. and J. Schultz: Nucleic Acid Metabolism of the Chromosomes in Relation to Gene Reproduction. Nature (London) 142, 294 (1938).
Casperrson, T. and B. Thorell: Der endozellulare Eiweiß-and NukleinsäureStoffwechsel im embryonalen Gewebe. Chromosoma 2, 132 (1941–1944).
Chantrenne, H.: The Requirement for Coenzyme A in the Enzymatic Synthesis of Hippuric Acid. J. biol. Chemistry 189, 227 (1951).
Cohen, P. P. and R. W. Mcgilvery: The Formation of p-Aminohippuric Acid by Rat Liver Slices. J. biol. Chemistry 266, 26, (1946).
Cohen, P. P. and R. W. Mcgilvery: Peptide Bond Synthesis. II. The Formation of p-Amino-hippuric Acid by Liver Homogenates. J. biol. Chemistry 169, 119 (1947).
Cohen, P. P. and R. W. Mcgilvery: Peptide Bond Synthesis. III. On the Mechanism of p-Aminohippuric Acid Synthesis J. biol. Chemistry 171, 121 (1947).
Cohen, S. S.: The Synthesis of Bacterial Viruses in Infected Cells. Cold Spring Harbor Sympos. _quantitat. Biol. 12, 35 (1947).
Collier, H. B.: The Problem of Plastein Formation. I. The Formation of Plastein by Papain. Canad. J. Res. Sect. B 18, 255 (1940).
Collier, H. B.: The Chemical Changes Involved in Plastein Formation by Papain and by Pepsin. Canad. J. Res. Sect. B 28, 272 (1940).
Cotzias, G. C. and V. P. Dole: Metabolism of Amines. II. Mitochondria) Localization of Monoamine Oxidase. Proc, Soc. exp. Biol. Med. 78, 157 (1951).
Cross, R. J., J. V. Taggart, G. A. Covo and D. E. Green: Studies on the Cyclophorase System. VI. The Coupling of Oxidation and Phosphorylation. J. biol. Chemistry 177, 655 (1949)
Cunningham, L., A. C. Griffinand J. M. Luck: Effect of a Carcinogenic Azo Dye on Liver Cell Structure. Isolation of Nuclei and Cytoplasmic Granules. Cancer Res. 10, 194 (1950).
Dovinsos, J. N.: Some Factors Influencing the Nucleic Acid Content of Cells and Tissues. Cold Spring Harbor Sympos. quantitat. Biol. 12, 50 (1947).
Delwiche, C. C., W. D. Loomisand P. K. Stumpf: Amide Metabolism in Higher Plants. II. The Exchange of Isotopic Ammonia by Glutamyl Transferase. Arch. Biochemistry 33, 333 (1951).
Ecker, P. G. E.: The Ultracentrifuge Study of Plastein. J. gen. Physiol. 30, 399 (1946)
Elliott, D. F. and A. Neuberger: Irreversibility of the Deamination of Threonine in the Rabbit and Rat. Biochemic. J. 46, 207 (1950).
Elliott, W. H.: Adenosinetriphosphate in Glutamine Synthesis. Nature (London) 161, 728 (1948).
Elliott, W. H.: Adenosinetriphosphate in Glutamine Synthesis. Biochemic. J. 42, V (1948).
Folin, O.: A Theory of Protein Metabolism. Amer. J. Physiol. 73, 117 (1905).
Folin, O. and W. Denis: Protein Metabolism from the Standpoint of Blood and Tissue Analyses. J. biol. Chemistry 11, 87 (1912).
Folley, S. J.: Note on the Preparation and Fractionation of the a-Naphthylisocyanate Compoand of Plastein. Biochemic. J. 27, 151 (1933)
Forker, L. L., L L. Charkoff, C. Entenmanand H. Tarver: Formation of Muscle Protein in Diabetic Dogs, Studied with S38-Methionine. J. biol. Chemistry 188, 37 (1951)
Frantz. I. D., Jr. and R. B. Loatfield: Equilibrium and Exchange Reactions Involving Peptides, Amino Acids, and Proteolytic Enzymes. Federat. Proc. (Amer. Soc. exp. Biol.) 9, 172 (1950).
Eitanrj, I. D., Jr., R. B. Loftfieldand W. W. Miller. Incorporation of C’ from Carboxyl-Labeled DL-Alanine into the Proteins of Liver Slices. Science (New York) 106, 544, (1947).
Frantz, I. D., Jr., P. C. Zamecnik, J. W. Reeseand M. L. Stephenson: The Effect of Dinitrophenol on the Incorporation of Alanine Labeled with Radioactive Carbon into the Proteins of Slices of Normal and Malignant Rat Liver. J. biol. Chemistry 174, 773 (1948).
Friedberg, F.: The Action of Dehydrocorticosterone in the Regulation of Protein Turnover Studied with Ss5 Labeled Methionine. Euclides 109, 116 (1950).
Friedberg, F. and D. M. Greenberg: The Effect of Growth Hormone on the Incorporation of 585 of Methionine into Skeletal Muscle Protein of Normal and Hypophysectomized Animals. Arch. Biochemistry 17, 193 (1948).
Friedberg, F., M. P. Schulmanand D. M. Greenberg: The Effect of Growth on the Incorporation of Glycine Labeled with Radioactive Carbon into the Protein of Liver Homogenates. J. biol. Chemistry 173, 437 (1948).
Friedberg, F., H. Tarverand D. M. Greenberg: The Distribution Pattern of Sulfur-Labeled Methionine in the Protein and the Free Amino Acid Fraction of Tissues after Intravenous Administration. J. biol. Chemistry 173, 355 (1948).
Fruton, J. S.: Rôle of Proteolytic Enzymes in Biosynthesis of Peptide Bonds. Yale J. Biol. Med. 22, 263 (1950).
Geiger, E.: Experiments with Delayed Supplementation of Incomplete Amino Acid Mixtures. J. Nutrit. 34, 97 (1947).
Geiger, E.: The Rôle of the Time Factor in Feeding Supplementary Proteins. J. Nutrit. 36, 813 (1948).
Geiger, E.: The Importance of the Time Element in Feeding of Growing Rats: Experiments with Delayed Supplementation of Protein. Science (New York) 108, 42 (1948).
Geiger, E.: The Rôle of the Time Factor in Protein Synthesis. Science (New York) 111, 594 (1950).
Geiger, E.: Extra Caloric Function of Dietary Components in Relation to Protein Utilization. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 670 (1951).
Geiger, E., E. B. Hagertyand H. D. Gatchell: Transformation of Tryptophan to Nicotinic Acid Investigated with Delayed Supplementation of Tryptophan Arch. Biochemistry 23, 315 (1949).
Greenberg, D. M., F. Friedberg, M. P. Schulmanand T. Winnick: Studies on the Mechanism of Protein Synthesis with Radioactive Carbon-Labeled Compoands Cold Spring Harbor Sympos. quantitat. Biol. 13, 113 (1948).
Greenberg, D. M. and T. Winnick: Studies in Protein Metabolism with Compoands Labeled with Radioactive Carbon. II. The Metabolism of Glycine in the Rat. J. biol. Chemistry 173, 199 (1948).
Greene, C. H.: Changes in Nitrogenous Extractives in the Muscular Tissue of the King Salmon During the Fast of Spawning Migration. J. biol. Chemistry 39, 457 (1919).
Griffin, A. C., S. Bloom, L. Cunningham, J. D. Teresiand J. M. Luck: The Uptake of Labeled Glycine by Normal and Cancerous Tissues in the Rat. Cancer 3, 316 (1950).
Grossowicz, N., E. Wainfan, E. Borekand H. Waelsch: The Enzymatic Formation of Hydroxamic Acids from Glutamine and Asparagine. J. biol. Chemistry 187, 111 (1950).
Hanes, C. S., F. J. R. Hirdand F. A. Isherwood: Synthesis of Peptides in Enzymatic Reactions Involving Glutathione. Nature (London) 166, 288 (1950).
Harte, R. A., J. J. Traversand P. Sarich: The Effect on Rat Growth of Alternated Protein Intakes. J. Nutrit. 35, 287 (1948).
Haugaard, G. and R. M. Roberts: Heats of Organic Reactions. XIV. The Digestion of ß-Lactoglobulin by Pepsin. J. Amer. chem. Soc. 64, 2664 (1942).
Henderson, R. and R. S. Harris: Concurrent Feeding of Amino Acids. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 385 (1949)
Herbst, R. M. and D. Shemin: The Synthesis of Peptides by Transamination. J. biol. Chemistry 147, 541 (1943)
Hitchcock, D.: Amphoteric Properties of Amino Acids and Proteins. In: C. L. A. Schmidt, Chemistry of the Amino Acids and Proteins, p. 596. Springfield, III. — Baltimore. 1938.
Hoberman, H. D.: Measurement of Rates of Protein Degradation and Protein Loss in Fasting Animals. J. biol. Chemistry 188, 797 (1951).
Hogeboom, G. H.: Separation and Properties of Cell Components. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 640 (1951)
Hogeboom, G. H. and W. C. Schneider: Cytochemical Studies of Mammalian Tissues. III. Isocitric Dehydrogenase and Triphosphopyridine Nucleotide-Cytochrome C Reductase of Mouse Liver. J. biol. Chemistry 186, 417 (1950).
Holloway, B. J. and S. H. Ripley: Nucleic Acid Content of Reticulocytes and its Relation to Uptake of Radioactive Leucine In Vitro. J. biol. Chemistry 196. 695, (1952).
>Hydén, H.: Protein Metabolism in the Nerve Cell and Reproduction. Acta physiol. Scand. 6, Suppl. 17, 1 (1943).
Hydén, H.: The Nucleoproteins in Virus Reproduction. Cold Spring Harbor Sympos. quantitat. Biol. 12, 104 (1947).
Johnston, R. B. and K. Bloch: Enzymatic Synthesis of Glutathione. J biol. Chemistry 188, 221 (1951).
Johnston, R. B., M. J. Mycekand J. S. Fruton: Catalysis of Transamidation Reactions by Proteolytic Enzymes. J. biol. Chemistry 185, 629 (1950).
Johnston, R. B., M. J. Mycekand J. S. Fruton: Catalysis of Transamidation Reactions by Chymotrypsin. J. biol. Chemistry 182, 205 (1950).
Kaufman, S. and H. Neurath: Inhibition of Chymotrypsin by Structural Analogs of Specific Substrates. Arch. Biochemistry 21, 245 (1940)
Kaufman, S. and H. Neurath: Structural Requirements of Specific Substrates for Chymotrypsin. II. An Analysis of the Contribution of the Structural Components to Enzymatic Hydrolysis. Arch. Biochemistry 21, 437 (1949)
Kaufman, S., H. Neurathand G. W. Schwert: The Specific Peptidase and Esterase Activities of Chymotrypsin. J. biol. Chemistry 177, 793 (1949)
Keller, E. B.: Turnover of Proteins of Cell Fractions of Adult Rat Liver In Vivo. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 206 (1951).
Kemen, A. J., S. W. Hunter, G. E. Mooreand C. R. Hitchcock: Distribution of Tracer Doses of Methionine Tagged with Radiosulfur in Normal and Neo-plastic Tissue. Cancer Res. 9, 174 (1949).
Feston, A. and J.-C. Dreyfus: Tracer Studies in Protein Synthesis: Antibody Formation by Spleen Slices. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 206 (1951).
Kielley, R. K. and W. C. Schneider: Synthesis of p-Aminohippuric Acid by Mitochondria of Mouse Liver Homogenates. J. biol. Chemistry 185, 869 (1950)
Kochakian, C. D.: The Protein Anabolic Effects of Steroid Hormones. Vitamins and Hormones 4, 255 (1946).
Kochakian, C. D.: The Effect of Dose and Nutritive State on the Renotrophic and Androgenic Activities of Various Steroids. Amer. J. Physiol. 145, 549 (1946).
Kochakian, C. D.: Comparison of Protein Anabolic Property of Various Androgens in the Castrated Rat. Amer. J. Physiol. 160, 83 (1950).
Kochakian, C. D.: Comparison of Protein Anabolic Properties of Testosterone Propionate and Growth Hormone in the Rat. Amer. J. Physiol. 160, 66 (1950)
Kochakian, C. D. and B. Beall: Comparison of the Protein Anabolic Property of Testosterone Propionate in the Male and Female Rat. Amer. J. Physiol. 160, 62 (1950).
Kochakian, C. D., J. H. Hammand M. N. Bartlett: Effect of Steroids on the Body Weight, Temporal Muscle and Organs of the Guinea Pig. Amer. J. Physiol. 155, 242 (1948).
Kochakian, C. D., J. G. Moeand J. Dolphin: Protein Anabolic Property of Testosterone Propionate in Adrenalectomized and Normal Rats. Amer. J. Physiol. 162, 581 (1950).
Le Page, G. A. and C. Heidelberger: Incorporation of Glycine-2-C“ into Proteins and Nucleic Acids of Normal and Neoplastic Rat Tissues. Federat. Proc. (Amer. Soc. exp. Biol.) 9, 195 (1950).
Le Page, G. A. and C. Heidelberger: Incorporation of Glycine-2-C14 into the Proteins and Nucleic Acids of the Rat. J. biol. Chemistry 188, 593 (1951).
Levine, M. and H. Tarver: On the Synthesis and some Applications of Serine-ß-C14. J. biol. Chemistry 184, 427 (1950).
Levine, M. and H. Tarver: Studies on Ethionine. III. Incorporation of Ethionine into Rat Proteins. J. biol. Chemistry 192, 835 (1951).
Li, C. H. and H. M. Evans: The Properties of the Growth and Adrenocorticotrophic Hormones. Vitamins and Hormones 5, 197 (1947)
Lipmann, F.: MetabolicGeneration and Utilization of Phosphate Bond Energy. Adv. Enzymology 1, 99 (1941).
Lipmann, F.: Mechanism of Peptide Bond Formation. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 597 (1949).
Litwack, G., J. N. Williams, Jr., F. Feigelsonand C. A. Elvehjem: Xanthine Oxidase and Liver Nitrogen Variation with Dietary Protein. J. biol. Chemistry 187, 605 (1950).
Loomis, W. F. and F. Lipmann: Reversible Inhibition of the Coupling between Phosphorylation and Oxidation. J. biol. Chemistry 173, 807 (1948).
Lotspeich, W. D.: Relations between Insulin and Pituitary Hormones in Amino Acid Metabolism. J. biol. Chemistry 185, 221 (1950).
Martin, C. J. and R. Robison: The Minimum Nitrogen Expenditure of Man and the Biological Value of Various Proteins for Human Nutrition. Biochemic. J. 16, 407 (1922).
Mcgilvery, R. W. and P. P. Cohen: Enzymatic Synthesis of Ornithuric Acids. J. biol. Chemistry 183, 179 (1950).
Melchior, J. B., O. Kliozeand I. M. Klotz: Further Studies of the Synthesis of Protein by Escherichia Coli. J. biol. Chemistry 189, 411 (1951).
Melchior, J. B., M. Mellodyand I. M. Klotz: The Synthesis of Protein by Non-proliferating Escherichia Coli. J. biol. Chemistry 174, 81 (1948).
Melchior, J. B. and H. Tarver: Studies in Protein Synthesis In Vitro. I. On the Synthesis of Labeled Cystine (Su) and its Attempted Use as a Tool in the Study of Protein Synthesis. Arch. Biochemistry 12, 301 (1947).
Melchior, J. B. and H. Tarver: Studies on Protein Synthesis In Vitro. II. On the Uptake of Labeled Sulfur by the Proteins of Liver Slices Incubated with Labeled Methionine (S25). Arch. Biochemistry 12. 309 (1947)
Miller, L. L.: Changes in Rat Liver Enzyme Activity with Acute Inanition. Relation of Loss of Enzyme Activity to Liver Protein Loss. J. biol. Chemistry 172, 113 (1948).
Miller, L. L.: The Loss and Regeneration of Rat Liver Enzymes Related to Diet Protein. J. biol. Chemistry 186, 253 (1950).
Muntwyler, E., S. Seifterand D. M. Harkness: Some Effects of Restriction of Dietary Protein on the Intracellular Components of Liver. J. biol. Chemistry 184, 181 (1950).
Northrop, J.: Plastein Formation from Pepsin,and Trypsin. J. gen. Physiol. 30, 377 (1946)
Peters, T., Jr. and C. B. Anfinsen: The Production of Radioactive Serum Albumin by Liver Slices. J. biol. Chemistry 182, 171 (1950).
Peters, T., Jr. and C. B. Anfinsen: Net Production of Serum Albumin by Liver Slices. J. biol. Chemistry 286, 805 (1950).
Peterson, E. A., D. M. Greenbergand T. Winnick: Characteristics of the Amino Acid Incorporation System of Liver Homogenates. Federat. Proc. (Amer. Soc. exp. Biol.) 9, 214 (1950).
Porter, R. R. and F. Sanger: The Free Amino Groups of Haemoglobin. Biochemic. J. 42, 287 (1948)
Potter, V. R.,, R. O. Recknageland R. B. Hurlbert: Intracellular Enzyme Distribution; Interpretations and Significance. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 646 (1951).
Price, J. M., E. C. Millerand J. A. Miller, The Intracellular Distribution of Protein, Nucleic Acids, Riboflavin and Protein-Boand Aminoazo Dye in the Livers of Rats Fed p-Dimethyl-aminoazobenzene. J. biol. Chemistry 173, 345 (1948)
Price, J. M., E. C. Miller, J A Millerand G. M. Weber: Studies On the Intracellular Composition of Livers from Rats Fed Various Aminoazo Dyes. I. 4-Aminoazobenzene, 4-Dimethylaminoazobenzene, 4’-Methyl and 3’-Methyl4-Dimethylaminoazobenzene. Cancer Res. 9, 398 (1949)
Price, J. M., E. C. Miller, J A Millerand G. M. Weber: Studies on the Intracellular Composition of Livers from Rats, Fed Various Aminoazo Dyes. II. 3’-Methyl-2’-Methyl-, and 2-Methyl-4-Dimethylaminoazobenzene, 3-Methyl-4-Monomethylaminoazobenzene, and 4’-Fluoro-4-Dimethylaminoazobenzene. Cancer Res. 10, 18 (1950).
Price, J. -M., J. A. Miller, E. C. Millerand G. M. Weber: Studies on the Intracellular Composition of Liver and Liver Tumor from Rats Fed 4-Dimethylaminoazo-benzene. Cancer Res. 9, 96 (1949)
Ratner, S., M. Blanchard, A. F. Coburnand D. E. Green: Isolation of a Peptide of p-Aminobenzoic Acid from Yeast. J. biol. Chemistry 155, 689 (1944)
Reid, J. C. and H. B. Jones: Radioactivity Distribution in the Tissues of Mice Bearing Melanosarcoma after Administration of DL-Tyrosine Labeled with Radioactive Carbon. J. biol. Chemistry 174, 427 (1948).
Reifenstein, E. C., F. Allbright, Jr. and S. L. Wells: Accumulation, Interpretation, and Presentation of Data Pertaining to Metabolic Balances, Notably Those of Calcium, Phosphorus, and Nitrogen. J. clin. Endocrin. 5, 367 (1945); Correction, ibid. 6, 232 (1946).
Rittenberg, D., R. Schoenheimer and A. S. Keston: Studies in Protein-Metabolism. IX. The Utilization of Ammonia by Normal Rats on a Stock Diet. J. biol. Chemistry 128, 603 (1939).
Rittenberg, D. and D. Shemin: The Metabolism of Proteins and Amino Acids. Annu. Rev. Biochem. 15, 247 (1946).
Rutman, R., E. Dempsterand H. Tarver: Genetic Differences in Methionine Uptake by Surviving Tissues. J. biol. Chemistry 177, 491 (1949)
Salter, W. T. and O. H. Pearson: The Enzymatic Synthesis from Thyroid Diiodotyrosine Peptone of an Artificial Protein which Relieves Myxedema. J. biol. Chemistry 112, 579 (1935/36).
Sanadi, D. R. and D. M. Greenberg: Effect of Amino Acid Deficiencies on Incorporation of Radioactive-Carbon Labeled Amino Acids into Animal Proteins. Proc. Soc. exp. Biol. Med. 69, 162 (1948).
Sarkar, N., M. Fuldand D. E. Green: Studies on the Synthesis of Hippuric Acid. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 242 (1951).
Schaeffer, A. J. and E. Geiger: Cataract Development in Animals with Delayed Supplementation of Tryptophane. Proc. Soc. exp. Biol. Med. 66, 309 (1947)
Schneider, W. C.: NucleicAcids in Normal and Neoplastic Tissues. Cold Spring Harbor Sympos. quantitat. Biol. 12, 169 (1947).
Schoenheimer, R.: The Dynamic State of Body Constituents. Cambridge, Mass.: Harvard Univ. Press. 1942.
Schoenheimer, R., S. Ratnerand D. Rittenberg: Studies in Protein Metabolism. VII. The Metabolism of Tyrosine. J. biol. Chemistry 127, 333 (1939).
Schoenheimer, R., S. Ratnerand D. Rittenberg: Studies on Protein Metabolism. X. The Metabolic Activity of Body Proteins Investigated with L(-) Leucine Containing Two Isotopes. J. burl. Chemistry 130, 703 (1939)
Schoenheimer, R., S. Rather, D. Rittenbergand M. Heidelberger: The Interaction of Blood Proteins of the Rat with Dietary Nitrogen. J. biol. Chemistry 144, 541 (1942).
Schou, M., N. Grossowicz, A. Lajthaand H. Waeish: Enzymatic Formation of Glutamo-Hydroxamic Acid from Glutamine in Mammalian Tissue, Nature (London) 167, 818 (1951).
Schwert, R. S.: (unpublished).
Schweigert, B. S., B. T. Guthneck, J. M. Price, J. A. Millerand E. C. MillerAmino Acid Composition of Morphological Fractions of Rat Livers and Induced Liver Tumors. Proc. Soc. exp. Biol. Med. 72, 495 (1949)
Schweigert, B. S., H. E. Sauberlich, C. A. Elvehjemand C. A. Baumann: Free Tryptophane in Blood and Urine. J. biol. Chemistry 164, 213 (1946).
Schwert, G. W., H. Neurath, S. Kaufmanand J. E. Snobe: The Specific Esterase Activity of Trypsin. J. biol. Chemistry 172, 221 (1948).
Seifter, S., E. Muntwylerand. D. M. Harkness: Some Effects of Continued Protein Deprivation, with and without Methionine Supplementation, on Intracellular Liver Components. Proc. Soc. exp. Biol. Med. 75, 46 (1950).
Shemin, D., J. M. Londonand D. Rittenberg: The Synthesis of Protoporphyrin In Vitro by Red Blood Cells of the Duck. J. biol. Chemistry 183, 757 (1950)
Shemin, D. and D. Rittenberg: Some Interrelationships in General Nitrogen Metabolism. J. biol. Chemistry 153, 401 (1944)
Siesevitz, P. and P. C. Zamecnik: In Vitro Incorporation of x-C“-DL-Alanine into Protein of Rat-Liver Granular Fractions Federat. Proc. (Amer Soc. exp.Biol.) 10, 246 (1951).
Simmonds, S., E. L. Tatumand J. S. Fruton: The Utilization of Phenyl-alanine and Tyrosine Derivatives by Mutant Strains of Escherichia Coli. J. biol. Chemistry 169, 91 (1947).
Simpson, M. V., E. Farberand H. Tarver: Studies on Ethionine: Inhibition of Protein Synthesis in Intact Animals J biol. Chemistry 182, 81 (1950).
Smith, E. L.: Catalytic Action of Metal Peptidases. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 581 (1949).
Snore, J. E. and H. Neurath: Structural Requirements of Specific Substrates for Chymotrypsin. I. The Contribution of the Secondary Peptide Group. Arch. Biochemistry 21, 351 (1949)
Snoke, J. E. and F. Rothman: Glutathione Synthesis from Glutamyl Cysteine and Glycine. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 249 (1951).
Speck, J. F.: The Enzymatic Synthesis of Glutamine. J. biol. Chemistry 168, 403 (1947)
Speck, J. F.: The Synthesis of Glutamine in Pigeon Liver Dispersions. J. biol. Chemistry 179, 1387 (1949)
Speck, J. F.: The Enzymatic Synthesis of Glutamine; A Reaction Using Adenosine Triphosphate. J. biol. Chemistry 179, 1405 (1949).
Spector, H. and H. H. Mitchell: Paired Feeding in the Study of the Counteraction by Nicotinic Acid and Tryptophane of the Growth-Depressing Effect of Corn in Rats. J. biol. Chemistry 165, 37 (1946).
Spiegelman, S. and M. D. Kamen: Genes and Nucleoproteins in the Synthesis of Enzymes. Science (New York) 104, 581 (1946).
Spiegelman, S. and M. D. Kamen: Some Basic Problems in the Relation of Nucleic Acid Turnover in Protein Synthesis. Cold Spring Harbor Sympos. quantitat. Biol. 12, 211 (1947)
Sprinson, D. B. and D. Rittenberg: The Rate of Utilization of Ammonia for Protein Synthesis. J. biol. Chemistry 180, 707 (1949).
Sprinson, D. B. and D. Rittenberg: The Rate of Interaction of the Amino Acids of the Diet with the Tissue Proteins. J. biol. Chemistry 180, 715 (1949).
Stumpf, P. K. and W. D. Loomis: Observations on a Plant Amide Enzyme System Requiring Manganese and Phosphate. Arch. Biochemistry 25, 451 (1950).
Stumpf, P. K., W. D. Loomisand C. Michelson, Amide Metabolism in Higher Plants. I. Preparation and Properties of Glutamyl Transferase from Pumpkin Seedling. Arch. Biochemistry 30, 126 (1951).
Tarver, H. and W. O. Reinhardt: Methionine Labeled with Radioactive Sulfur as an Indicator of Protein Formation in the Hepatectomized Dog. J. biol. Chemistry 167, 395 (1947)
Tarver, H. and C. L. A. Schmidt: Radioactive Sulfur Studies. I. Synthesis of Methionine. II. Conversion of Methionine Sulfur to Taurine Sulfur in Dogs and Rats. III. Distribution of Sulfur in the Proteins of Animals Fed Sulfur or Methionine. IV. Experiments In Vitro with Sulfur and Hydrogen Sulfide. J. biol. Chemistry 146, 69 (1942).
Tauber, H. T.: Protein Synthesis by Chymotrypsin. J. Amer. chem. Soc 71, 2952 (1949)
Tauber, H. T.: Synthesis of High Molecular-Weight Protein-Like Substances by Chymotrypsin. Federat. Proc. (Amer. Soc. exp. Biol.) 9, 237 (1950).
Tauber, H. T.: Synthesis of Protein-Like Substances by Chymotrypsin. J. Amer. chem. Soc. 73, 1288 (1951).
Tauber, H. T.: Synthesis of Protein-Like Substances by Chymotrypsin from Dilute Peptic Digests and their Electrophoretic Patterns. J. Amer. chem. Soc. 73, 4965 (1951).
Thorell, B.: The Relation of Nucleic Acids to the Formation and Differentiation of Cellular Proteins. Cold Spring Harbor Sympos. quantitat. Biol. 12, 247 (1947)
Totter, J. R., B. Kelley, P. L. Dayand R. R. Edwards: The Metabolism of Glycine by Folic Acid-Deficient Chick Liver Homogenates. J. biol. Chemistry 186, 145 (1950).
Tyner, E. P., C. Heidelbergerand G. A. Le Page: Rates and Synthesis and Turnover of Proteins and Nucleic Acid Purines in the Rat. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 262 (1951).
Van Slyke, D. D. and G. M. Meyer: The Effects of Feeding and Fasting on the Amino Acid Content of the Tissues J. biol. Chemistry 16, 231 (1913).
Vendrely, C., R. Vendrely: L’acide ribonucléique des mitochondries et des microsomes du foie et ses variations au cours du jeûne protéique. C. R. hebd. Séances Acad. Sci. 230, 333 (1950).
Vierordt, H.: Anatomische, physiologische and physikalische Daten and Tabellen. Jena. 1906.
Virtanen, A. I. and H. K. Kerkkonen: On the Chemical Nature of Plasteins. Acta chem. Scand. 5, 140 (1947).
Virtanen, A. I. and H. K. Kerkkonen: Structure of Plasteins. Nature (London) 161, 888 (1948).
Virtanen, A. I., H. K. Kerkkonen, M. Hakalaand T. Laaksonen: Die Synthese von Polypeptiden durch die Wirkung von Pepsin. Naturwiss. 37. 139 (1950).
Virtanen, A. I., H. K. Kerkkonen, T. Laaksonenand M. Hakala: Plastein, a Mixture of Higher-Molecular Polypeptides Synthesized by Proteolytic Enzymes. Acta chem. Scand. 3, 520 (1949).
Waelsch, H.: Glutamotransferase Activity in Mammalian Tissue Extracts. Federat. Proc. (Amer. Soc. exp. Biol.) 10, 266 (1951).
Waelsch, H.: Glutamic Acid and Cerebral Function. Adv. Protein Chem. 6, 299 (1951).
Waelsch, H., E. Borek, N. Grossowiczand M. Scxou: Glutamo-and AspartoTransferases. Federat. Proc. (Amer. Soc. exp. Biol.) 9, 242 (1950).
Waelsch, H., P. Owades, E. Borek, N. Grossowiczand M. Scxou: The Enzyme-Catalyzed Exchange of Ammonia with the Amide Group of Glutamine and Asparagine. Arch. Biochemistry 27, 237 (1950).
Waelsch, H. and D. Rittenberg: Glutathione. II. The Metabolism of Glutathione Studied with Isotopic Ammonia and Glutamic Acid. J. biol. Chemistry 144, 53 (1942).
Waldschmidt-Leitz, E. and K. Kühn: Über die enzymatische Synthese von Peptidbindungen. Hoppe-Seyler’s Z. physiol. Chem. 285, 22 (1950).
Wasteneys, H. and H. Boasook: The Enzymatic Synthesis of Protein. Physiologic. Rev. 10, 110 (1930).
Weissman, N. and R. Schoenheimer: The Relative Stability of L(+) Lysine in Rats Studied with Deuterium and Heavy Nitrogen. J. biol. Chemistry 140, 779 (1941).
Westerfield, W. W. and D. A. Richert: Dietary Effects on Liver Xanthine Oxidase. Federat. Proc. (Amer. Soc. exp. Biol.) 8, 265 (1949).
Williams, J. N., Jr. and C. A. Elvehjem: The Relation of Amino Acid Availability in Dietary Protein to Liver Enzyme Activity. J. biol. Chemistry 181, 559 (1949)
Winnick, T.: Studies on the Mechanism of Protein Synthesis in Embryonic and Tumor Tissues. I. Evidence Relating to the Incorporation of Labeled Amino Acids into Protein Structure in Homogenates. Arch. Biochemistry 27, 65 (1950).
Winnick, T.: Studies on the Mechanism of Protein Synthesis in Embryonic and Tumor Tissues. II. Inactivation of Fetal Rat Liver Homogenates by Dialysis, and Reactivation by the Adenylic Acid System. Arch. Biochemistry 28, 338 (1950).
Winnick, T., F. Friedberg and D. M. Greenberg: Incorporation Of C14-Labeled Glycine into Intestinal Tissue and its Inhibition by Azide. Arch. Biochemistry 55, 160 (1947)
Winnick, T., F. Friedbergand D. M. Greenberg: Studies in Protein Metabolism with Compoands Labeled with Radioactive Carbon. I. Metabolism of DL-Tyrosine in the Normal and Tumor-Bearing Rat. J. biol. Chemistry 173, 189 (1948).
Winnick, T., F. Friedbergand D. M. Greenberg: The Utilization of Labeled Glycine in the Process of Amino Acid Incorporation by the Protein of Liver Homogenate. J. biol. Chemistry 175, 117 (1948).
Winnick, T., E. A. Petersonand D. M. Greenberg: Incorporation of C14-Glycine into Protein and Lipide Fractions of Homogenates. Arch. Biochemistry 21, 235 (1949).
Woodward, G. E.: S85-Glutathione Preparation from Yeast and Tracer Studies in Cancerous and Non-Cancerous Rats. J. Franklin Inst. 251, 557 (1951).
Work, T. S. and E. Work: The Basis of Chemotherapy, p. 227. New York: Interscience Publ. 1948.
Yeshoda, K. M. and M. Damodaran: Amino-Acids and Proteins in Haemoglobin Formation. Biochemic. J. 41, 382 (1947).
Zamecnik, P. C.: The Use of Labeled Amino Acids in the Study of the Protein Metabolism of Normal and Malignant Tissues: A Review. Cancer Res. 10, 659 (1950)
Zamecnik, P. C. and I. D. Frantz, Jr.: Peptide Bond Synthesis in Normal and Malignant Tissue. Cold Spring Harbor Sympos. quantitat. Biol. 14, 199 (1949)
Zamecnik, P. C., I. D. Frantz, Jr., R. B. Loftfieldand M. L. Stephenson: Incorporation In Vitro of Radioactive Carbon from Carboxyl-Labeled DL-Alanine and Glycine into Proteins of Normal and Malignant Rat Livers. J. biol. Chemistry 175, 299 (1948).
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Borsook, H. (1952). The Biosynthesis of Proteins and Peptides, including Isotopic Tracer Studies. 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/Progrès Dans La Chimie Des Substances Organiques Naturelles, vol 9. Springer, Vienna. https://doi.org/10.1007/978-3-7091-7169-1_7
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