NDLI: A potent, heat-stable protein inhibitor of [branched-chain alpha-keto acid dehydrogenase]-phosphatase from bovine kidney mitochondria.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Reed, L. J. Damuni, Z. Humphreys, J. S.
Abstract	A heat- and acid-stable protein inhibitor of the [branched-chain alpha-keto acid dehydrogenase]-phosphatase was purified over 100,000-fold from extracts of bovine kidney mitochondria. The nearly homogeneous protein was recovered with a yield of 4-8%. The apparent molecular weight of the inhibitor is about 36,000. This protein is a noncompetitive inhibitor of the phosphatase, and the inhibitor constant (Ki) is about 0.13 nM. The inhibition was reversed 50% by about 1.3 mM Mg2+ and about 0.1 mM spermine. This protein inhibitor is different from the cytosolic protein phosphatase inhibitors 1 and 2.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acids, Branched-Chain Metabolism Enzyme Inhibitors Isolation & Purification Ketone Oxidoreductases Mitochondria Enzymology Multienzyme Complexes Protein Kinase Inhibitors Protein Kinases 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Animals Hot Temperature Kidney Magnesium Pharmacology Molecular Weight Spermine Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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A potent, heat-stable protein inhibitor of [branched-chain alpha-keto acid dehydrogenase]-phosphatase from bovine kidney mitochondria.