PMID: 3768411Oct 29, 1986Paper

Activation of hepatic branched-chain 2-oxoacid dehydrogenase by rat liver cytosolic supernatant

Biochimica Et Biophysica Acta
S Hauschildt

Abstract

Hepatic branched-chain 2-oxoacid dehydrogenase is inactivated by nutritional alterations. Reactivation occurs during preincubation of intact mitochondria in the presence of rat liver cytosolic supernatant. Cytosolic supernatant contains two factors capable of reactivating the enzyme. On gel-filtration (Sephadex G-100), one factor (AF1) elutes in the molecular range of 35,000-40,000 and the other factor (AF2) elutes slightly later than inorganic phosphate. AF2 is stable against heat denaturation and treatment with proteinases. It is destroyed by alkaline phosphatase and in the presence of Ap5A, atractyloside, CaCl2 and NaF its stimulatory effect on branched-chain 2-oxoacid dehydrogenase activity is abolished. Inhibition of activation by NaF suggests that a phosphatase might be involved in the activation process.

References

Jun 1, 1978·The Biochemical Journal·P J Parker, P J Randle
Mar 1, 1977·The Journal of Clinical Investigation·B S KhatraD Rudman
Feb 15, 1979·The Biochemical Journal·R Odessey, A L Goldberg
Jun 1, 1978·FEBS Letters·P J Parker, P J Randle
Jan 1, 1976·Analytical Biochemistry·A Bensadoun, D Weinstein

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