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Metabolism of ε-(γ-L-glutamyl)-L-lysine in the rat

Published online by Cambridge University Press:  09 March 2007

G. Raczyński
Affiliation:
Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jablonna, near Warsaw, Poland
M. Snochowski
Affiliation:
Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jablonna, near Warsaw, Poland
S. Buraczewski
Affiliation:
Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, 05-110 Jablonna, near Warsaw, Poland
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Abstract

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1. A study was made of the metabolism of ɛ-(γ-L-glutamyl)-L[4, 5-3H]lysine (GL) in the rat.

2. The compound was largely absorbed from the intestine and metabolized. Labelled lysine was incorporated into blood proteins.

3. In an in vitro experiment with everted sacs of rat small intestine, GL passed through the intestinal wall unchanged.

4. The results of comparative tests using homogenates of different body tissues indicated that the kidneys were particularly active in hydrolysing GL. Their activity was nine times greater than that of the liver and eighteen times greater than that of the small intestine.

Type
Papers of direct relevance to Clinical and Human Nutrition
Copyright
Copyright © The Nutrition Society 1975

References

Bjarnason, J. & Carpenter, K. J. (1970). Br. J. Nutr. 24, 313.CrossRefGoogle Scholar
Carpenter, K. J. (1973). Nutr. Abstr. Rev. 43, 424.Google Scholar
Cohen, P. P. (1957). In Manometric Techniques, p. 147 [Jmbreit, W. WBurris, R. H and Stauffer, J. F, editors]Minneapolis: Burgess Publishing Co.Google Scholar
Crane, R. K. & Wilson, T. H. (1958). J. appl. Physiol. 12, 145.CrossRefGoogle Scholar
Ford, J. E. & Shorrock, C. K. (1971). Br. J. Nutr. 26, 311.Google Scholar
Leclerc, J. & Benoiton, L. (1968). Can. J. Biochem. Physiol. 46, 471.Google Scholar
Paik, W. K. & Benoiton, L. (1963). Can. J. Biochem. Physiol. 41, 1643.CrossRefGoogle Scholar
Paik, K. W., Bloch-Frankenthal, L., Birnbaum, S. M., Winitz, M. & Greenstein, J. P. (1957). Archs Biochem. Biophys. 69, 56.Google Scholar
Peacock, A. C. & Harris, R. S. (1950). Archs Biochem. 27, 198.Google Scholar
Raceski, G. & Buraczewski, S. (1973). Proc. int. Symp. Amino Acids, Brno, A20.Google Scholar
Stupnicki, R., Barcikowski, B. & Kwiatkowska, Z. (1971). Endokr. pol. 22, 393.Google Scholar
Waibel, P. E. & Carpenter, K. J. (1972). Br. J. Nutr. 27, 509.CrossRefGoogle Scholar
Zahn, H. & Patzold, W. (1963). Chem. Ber. 96, 2566.Google Scholar