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Adaptive enzyme changes in liver and muscle of rats during protein depletion and refeeding

Published online by Cambridge University Press:  09 March 2007

Joan M. L. Stephen
Joan M. L. Stephen
Affiliation:
Medical Research Council Tropical Metabolism Research Unit, University of the West Indies, Jamaica
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Abstract

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1. Young rats were kept on a 6% casein diet for 4–7 weeks and then either killed or returned to a stock diet. Control rats were given a stock diet.

2. Argininosuccinate lyase (EC 4.3.2.1, L-argininosuccinate arginine-lyase) was assayed in liver, and amino acid activating enzymes were assayed in liver and muscle of rats after depletion and while they were refed on the stock diet. Levels of enzymes were compared with those in the control rats.

3. Amino acid activating enzymes were markedly increased in liver at the end of the depletion period, but returned almost to normal levels after 4–6 days of refeeding. In muscle the enzyme levels were not decreased after depletion, but began to rise after 4 days of refeeding.

4. Argininosuccinate lyase activity in depleted female rats was about half that in control rats and rose again slowly on refeeding. Male rats were hardly affected by depletion.

5. It is suggested that these enzyme changes play a part in the adaptation of the rat to a reduced protein intake.

Type
Research Article
Information
British Journal of Nutrition , Volume 22 , Issue 2 , May 1968 , pp. 153 - 163
Copyright
Copyright © The Nutrition Society 1968

References

Alleyne, G. A. O. & Young, V. H. (1966). Lancet i, 911.CrossRefGoogle Scholar
Alleyne, G. A. O. & Young, V. H. (1967). Clin. Sci. 33, 189.Google Scholar
Barnes, R. H., Cunnold, S. R., Zimmermann, R. R., Simmons, H., MacLeod, R. B. & Krook, L. (1966). J. Nutr. 89, 399.CrossRefGoogle Scholar
Bendicenti, A., Mariani, A., Paolucci, A. M., & Spadoni, M. A. (1959). Boll. Soc. Biol. sper. 35, 1997.Google Scholar
Ceriotti, G. & Spandrio, L. (1963). Clinica chim. Acta 8, 295.CrossRefGoogle Scholar
De Moss, J. A. & Novelli, G. D. (1956). Biochim. biophys. Acta 22, 49.CrossRefGoogle Scholar
Durbin, P. A. J. & Heard, C. R. C. (1962). Proc. Nutr. Soc. 21, xxviii.Google Scholar
Fletcher, K. (1966). Am. J. clin. Nutr. 19, 170.CrossRefGoogle Scholar
Freedland, R. A. & Harper, A. E. (1959). J. biol. Chem. 234, 1350.CrossRefGoogle Scholar
Freedland, R. A. & Sodikoff, C. H. (1962). Proc. Soc. exp. Biol. Med. 109, 394.CrossRefGoogle Scholar
Gaetani, S., Mariani, A., Spadoni, M. A. & Tomassi, G. (1961). Boll. Soc. Biol. sper. 37, 1685.Google Scholar
Gaetani, S., Paolucci, A. M., Spadoni, M. A. & Tomassi, G. (1964). J. Nutr. 84, 173.CrossRefGoogle Scholar
Kiriyama, S. & Ashida, K. (1964). J. Nutr. 82, 127.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
McCorquodale, D. J. & Mueller, G. C. (1958). J. biol. Chem. 232, 31.CrossRefGoogle Scholar
McLean, P. & Gurney, M. W. (1963). Biochem. J. 87, 96.CrossRefGoogle Scholar
Mariani, A., Migliaccio, P. A., Spadoni, M. A. & Ticca, M. (1966). J. Nutr. 90, 25.CrossRefGoogle Scholar
Mariani, A., Spadoni, M. A. & Tomassi, G. (1963). Nature, Lond. 199, 378.CrossRefGoogle Scholar
Mendes, C. B. & Waterlow, J. C. (1958). Br. J. Nutr. 12, 74.CrossRefGoogle Scholar
Munro, H. N. (1964). In Mammalian Protein Metabolism. Vol. 1, chapter 10. [Munro, H. N. and Allison, J. B. editors.] New York and London: Academic Press Inc.Google Scholar
Pennington, R. J. (1960). Biochem. J. 77, 205.CrossRefGoogle Scholar
Radhakrishnan, M. R. (1966). Indian J. med. Res. 54, 486.Google Scholar
Schimke, R. T. (1962 a). J. biol. Chem. 237, 1921.CrossRefGoogle Scholar
Schimke, R. T. (1962 b). J. biol. Chem. 237, 459.CrossRefGoogle Scholar
Schimke, R. T. (1963). J. biol. Chem. 238, 1012.CrossRefGoogle Scholar
Smith, A. L., Koeppe, O. J. & Franz, J. M. (1961). Endocrinology 69, 872.CrossRefGoogle Scholar
Srinivasan, P. R. & Patwardhan, V. N. (1955). Indian J. med. Res. 43, 1.Google Scholar
Stenram, U. & Hirschman, R. (1965). Acta anat. 61, 445.CrossRefGoogle Scholar
Stephen, J. & Waterlow, J. C. (1968). Lancet i, 118.CrossRefGoogle Scholar
Taussky, H. H. & Shorr, E. (1953). J. biol. Chem. 202, 675.CrossRefGoogle Scholar
Waterlow, J. (1959). Nature, Lond. 184, 1875.CrossRefGoogle Scholar
Waterlow, J. C., Alleyne, G. A. O., Chan, H., Garrow, J. S., Hay, A., James, P., Picou, D. & Stephen, J. M. L. (1966). Archos lat.-am. Nutr. 16, 175.Google Scholar
Waterlow, J. C. & Stephen, J. M. L. (1966). Br. J. Nutr. 20, 461.CrossRefGoogle Scholar
Weber, G. & Singhal, R. L. (1964). J. biol. Chem. 239, 521.CrossRefGoogle Scholar