Abstract
Plasma membrane fractions from rat liver isolated by different methods contain NADH- ferricyanide reductase and NADH-semidehydroascorbate reductase activities which are too high to be due to contamination by mitochondria or microsomes. Both enzymes are inhibited by insulin in a concentration range of 30 to 70 μU insulin/ml down to 20% residual activity. While ferricyanide reductase returns to near normal activity, semidehydroascorbate reductase inhibition persists at higher insulin concentrations. Despite variations in basal enzyme activities, degree of inhibition and amount of hormone needed for maximal effect, it can be consistently observed. Inhibition of semidehydroascorbate reductase is discussed in terms of the enzyme's function in regenerating ascorbate as antioxidant and oxidant-like insulin effects.
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