The relationship between the rate of glutamate deamination and long-chain acyl-CoA accumulation in kidney cortex mitochondria of rabbit |
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Authors: | J M Dzik |
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Institution: | Institute of Biochemistry, University of Warsaw Al. Zwirki i Wigury 93, 02-089 Warsaw, Poland |
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Abstract: | The effect of long-chain acyl-CoA on glutamate dehydrogenase activity was studied in uncoupled rabbit kidney cortex mitochondria incubated with glutamate and palmitoylcarnitine in the presence of arsenite. The mitochondrial long-chain acyl-CoA (about 2 nmol/mg of protein) accumulated in the presence of arsenite resulted in an inhibition of ammonia production from 4.1 to 1.2 nmol/min per mg of protein. Leucine and ADP, activators of glutamate dehydrogenase, did not release the inhibitory effect of long-chain acyl-CoA on glutamate deamination. In view of the presented data it seems that inhibitory effect of long-chain acyl-CoA on glutamate dehydrogenase activity may have a physiological significance. |
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