Jun 1, 1991

Purification and properties of branched-chain alpha-keto acid dehydrogenase kinase from bovine kidney

BioFactors
H Y LeeL J Reed

Abstract

Branched-chain alpha-keto acid dehydrogenase (BCKDH) kinase was purified 5000-fold to apparent homogeneity from extracts of bovine kidney mitochondria. The kinase co-purified with the BCKDH complex. About 70% of the kinase was released by treatment of the complex with 1.5 M NaCl and 0.1% 2-mercaptoethanol at pH 7.4, followed by chromatography on Sephacryl S-400. The uncomplexed kinase was purified further by chromatography on Q Sepharose and Superose 12. The purified kinase is a monomer of apparent Mr approximately 43,000. BCKDH kinase exhibited little activity, if any, toward pyruvate dehydrogenase.

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Mentioned in this Paper

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
2-Mercaptoethanol
Pyruvate dehydrogenase
SDS-PAGE
Chromatography
Bos taurus
Kidney
Cattle Diseases
Mitochondria
Protein KINASE

About this Paper

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