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Department of Poultry Science and Graduate School of Nutrition, Cornell University, Ithaca, New York 14850
The factors influencing lysine degradation were investigated by studying the level of liver lysine-ketoglutarate reductase (the initial degradative enzyme) and the conversion of 14C-lysine to 14CO2 in the intact chick. Liver lysine-ketoglutarate reductase activity was increased by excesses of dietary lysine, but not arginine, and kidney arginase activity was increased by excesses of both arginine and lysine. The rate of 14CO2 production from 14C-lysine in vivo was correlated with the lysine-ketoglutarate reductase activity measured in vitro when a loading dose of lysine was given. No correlation was observed when a trace dose was given. The rate of lysine oxidation was stimulated by lysine, but excesses of dietary arginine did not increase lysine oxidation. Genetic differences in lysine-ketoglutarate reductase and the rate of 14C-lysine oxidation were observed between the high arginine and low arginine requirement strains. These findings suggest that the rate of lysine oxidation in vivo may be regulated by the lysine pool at low levels of dietary lysine, and by the level of degradative enzyme at high levels of dietary lysine.
KEY WORDS: lysine degradation lysine-ketoglutarate reductase arginase
1 Supported in part by Public Health Service Grants AM06850 and AM14187 from the National Institute for Arthritis and Metabolic Diseases.
Manuscript received 31 July 1972.
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