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Mechanisms of heat damage in proteins

3.* Studies with ɛ-(γ-L-glutamyl)-L-lysine

Published online by Cambridge University Press:  09 March 2007

P. E. Waibel  and
K. J. Carpenter
P. E. Waibel
Affiliation:
Department of Applied Biology, University of Cambridge
K. J. Carpenter
Affiliation:
Department of Applied Biology, University of Cambridge
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Abstract

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1. ε-(γ-L-Glutamyl)-L-lysine was found to have a growth-promoting activity that was approximately equal to the equivalent quantity of L-lysine for both young rats and chicks receiving a lysine-deficient diet.

2. Small quantities of the compound were found in the plasma of the chicks and rats receiving it at the level of 0.4–0.5% on the diet, but none was detected in the rat urine and only a trace in the separated chick urine.

3. Direct intravenous infusion of glutamyl-lysine into rats resulted in higher plasma concentrations; it is suggested that hydrolysis of the ingested peptides may occur largely in the intestinal wall.

4. The findings are discussed in relation to the earlier hypothesis that the formation of glutamyl-lysine cross-linkages in severely heated protein provides an explanation of their reduced nutritional value.

Type
General Nutrition
Information
British Journal of Nutrition , Volume 27 , Issue 3 , May 1972 , pp. 509 - 515
Copyright
Copyright © The Nutrition Society 1972

References

Asquith, R. S., Otterburn, M. S., Buchanan, J. H., Cole, M., Fletcher, J. C. & Gardner, K. L. (1970). Biochim. biophys. Acta. 221, 342.CrossRefGoogle Scholar
Bjarnason, J. & Carpenter, K. J. (1969). Br. J. Nutr. 23, 859.CrossRefGoogle Scholar
Bjarnason, J. & Carpenter, K. J. (1970). Br. J. Nutr. 24, 313.CrossRefGoogle Scholar
Burns, J. A., Curtis, C. F. & Kacser, H. (1965). J. Chromat. 20, 310.CrossRefGoogle Scholar
Carpenter, K. J., March, B. E., Milner, C. K. & Campbell, R. C. (1963). Br. J. Nutr. 17, 309.CrossRefGoogle Scholar
Dawson, R. & Porter, J. W. G. (1962). Br. J. Nutr. 16, 27.CrossRefGoogle Scholar
Finney, D. J. (1964). Statistical Methods in Biological Assay 2nd ed. New York: Hafner Publishing Co.Google Scholar
Ford, J. E. (1965). Br. J. Nutr. 19, 277.CrossRefGoogle Scholar
Leclerc, J. & Benoiton, L. (1968). Can. J. Biochem. 46, 471.CrossRefGoogle Scholar
Mauron, J. (1970). J. int. Vitaminol. 40, 209.Google Scholar
Miller, E. L., Carpenter, K. J. & Milner, C. K. (1965). Br. J. Nutr. 19, 547.CrossRefGoogle Scholar
Newberne, P. M., Laerdal, O. A. & O'Dell, B. L. (1957). Poult. Sci. 36, 821CrossRefGoogle Scholar
Paik, W. K. & Benoiton, L. (1963). Can. J. Biochem. Physiol. 41, 1643.CrossRefGoogle Scholar
Pisano, J. J., Finlayson, J. S. & Peyton, M. P. (1969). Biochemistry, Euston. 8, 871.CrossRefGoogle Scholar
Varnish, S. A. & Carpenter, K. J. (1970). Proc. Nutr. Soc. 29, 45A.Google Scholar