Hostname: page-component-cd9895bd7-8ctnn Total loading time: 0 Render date: 2024-12-26T07:51:33.802Z Has data issue: false hasContentIssue false

Amino Acid Imbalance*

Published online by Cambridge University Press:  28 February 2007

A. E. Harperand
Affiliation:
Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Q. R. Rogers
Affiliation:
Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
Rights & Permissions [Opens in a new window]

Abstract

Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Amino Acid Imbalance
Copyright
Copyright © The Nutrition Society 1965

Footnotes

*

This work was supported by Public Health Service Research Grant No. AM-05718 from the National Institute of Arthritis and Metabolic Diseases.

References

Benton, D. A., Harper, A. E., Spivey, H. E. & Elvehjem, C. A. (1956). Arch. Biochem. Biophys. 60, 147.CrossRefGoogle Scholar
Cannon, P. R., Steffee, C. H., Frazier, L. J., Rowley, D. A. & Stepto, R. C. (1947). Fed. Proc. 6, 390.Google Scholar
Deshpande, P. D., Harper, A. E. & Elvehjem, C. A. (1958). J. biol. Chem. 230, 335.CrossRefGoogle Scholar
Earle, D. P., Smull, K. & Victor, J. (1942 a). J. exp. Med. 75, 179.Google Scholar
Earle, D. P., Smull, K. & Victor, J. (1942 b). J. exp. Med. 75, 191.Google Scholar
Elman, R. (1939). Proc. Soc. exp. Biol., N.Y., 40, 484.CrossRefGoogle Scholar
Elvehjem, C. A. & Krehl, W. A. (1955). Borden's Rev. Nutr. Res. 16, 69.Google Scholar
Fisher, H. & Shapiro, R. (1961). J. Nutr. 75, 395.Google Scholar
Frazier, L. E., Wissler, R. W., Steffee, C. H., Woolridge, R. L. & Cannon, P. R. (1947). J. Nutr. 33. 65.CrossRefGoogle Scholar
Geiger, E. (1947). J. Nutr. 34, 97.Google Scholar
Greenstein, J. P. & Winitz, M. (1961). Chemistry of the Amino Acids. Vol. 1 p. 286. New York: Wiley.Google Scholar
Harper, A. E. (1958). Ann. N.Y. Acad. Sci. 69, 1025.Google Scholar
Harper, A. E. (1959). J. Nutr. 68, 405.CrossRefGoogle Scholar
Harper, A. E. (1964 a).In Mammalian Protein Metabolism. Vol. 2, p. 87. [Munro, H. N. and Allison, J. B.editors.] New York: Academic Press Inc.Google Scholar
Harper, A. E. (1964 b). In Mammalian Protein Metabolism. Vol. 2, p. 119. [Munro, H. N. and Allison, J. B.editors.] New York: Academic Press Inc.Google Scholar
Harper, A. E., Benton, D. A. & Elvehjem, C. A. (1955). Arch. Biochem. Biophys. 57, 1.CrossRefGoogle Scholar
Harper, A. E. & Kumta, U. S. (1959). Fed. Proc. 18, 1136.Google Scholar
Henderson, L. M., Koeppe, O. J. & Zimmerman, H. H. (1953). J. biol. Chem. 201. 697.Google Scholar
Jones, J. D. (1964). J. Nutr. 84, 313.Google Scholar
Klain, G. J. & Vaughn, D. A. (1963). Fed. Proc. 22, 862.Google Scholar
Klain, G. J., Vaughn, D. A. & Vaughn, L. N. (1962). J. Nutr. 78, 359.Google Scholar
Kumta, U. S., Elias, L. G. & Harper, A. E. (1961). J. Nutr. 73, 229.CrossRefGoogle Scholar
Kumta, U. S. & Harper, A. E. (1960). J. Nutr. 70, 141.Google Scholar
Kumta, U. S. & Harper, A. E. (1961). J. Nutr. 74, 139.CrossRefGoogle Scholar
Kumta, U. S. & Harper, A. E. (1962). Proc. Soc. exp. Biol., N.Y., 110, 512.Google Scholar
Kumta, U. S., Harper, A. E. & Elvehjem, C. A. (1958). J. biol. Chem. 233, 1505.CrossRefGoogle Scholar
Leung, P.,Rogers, Q. R. & Harper, A. E. (1964). Fed. Proc. 23, 185.Google Scholar
Lewis, D. (1965). Proc. Nutr. Soc. 24, 196.CrossRefGoogle Scholar
Longenecker, J. B. & Hause, N. L. (1959). Arch. Biochem. Biophys. 84, 46.Google Scholar
McLaughlan, J. M. & Morrison, A. B. (1965). In Significance of Changes in Plasma Amino Acid Patterns. [Leathem, J. M., editor]. New Brunswick N. J.: Rutgers University Press. (In the Press.)Google Scholar
Morrison, M. A. & Harper, A. E. (1960) J. Nutr. 71, 296.Google Scholar
Morrison, M. A., Reynolds, M. S. & Harper, A. E. (1960). J. Nutr. 72, 302.Google Scholar
Munaver, S. M. & Harper, A. E. (1959). J. Nutr. 69, 58.Google Scholar
Rogers, Q. R., Spolter, P. D. & Harper, A. E. (1962). Arch. Biochem. Biophys. 97, 497.CrossRefGoogle Scholar
Rosenberg, H. R.,Culik, R. & Eckert, R. E. (1959). J. Nutr. 69, 217.Google Scholar
Salmon, W. D. (1954). Arch. Biochern. Biophys. 51, 30.CrossRefGoogle Scholar
Salmon, W. D. (1958). Amer. J. clin. Nutr. 6, 487.Google Scholar
Sanahuja, J. C. & Harper, A. E. (1962). Amer. J. Physiol. 202, 165.CrossRefGoogle Scholar
Sanahuja, J. C. & Harper, A. E. (1963 a). Amer. J. Physiol. 204, 686.Google Scholar
Sanahuja, J. C. & Harper, A. E. (1963 b) J. Nutr. 81, 363.Google Scholar
Sauberlich, H. E. (1961). J. Nutr. 75, 61.Google Scholar
Sauberlich, H. E. & Salmon, W. D. (1955). J. biol. Chem. 214, 463.Google Scholar
Schweizer, W. (1947). J. Physiol. 106, 167.Google Scholar
Sidransky, H. & Baba, T. (1960). J. Nutr. 70, 463.Google Scholar
Sidransky, H. & Farber, E. (1958). Arch. Path. 66, 135.Google Scholar
Smith, G. H. & Lewis, D. (1964). Proc. Nutr. Soc. 23, xxviii.Google Scholar
Spolter, P. D. & Harper, A. E. (1961). Amer. J. Physiol. 200, 513.Google Scholar
Tarver, H. (1963). In The Liver. Vol. 1, p. 450. [Rouiller, C., editor]. New York: Academic Press Inc.Google Scholar
Waisman, H. A. & Harlow, H. F. (1965). Science, 147, 685.CrossRefGoogle Scholar