| Literature DB >> 1910451 |
H Y Lee1, T B Hall, S M Kee, H Y Tung, L 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.Entities:
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Year: 1991 PMID： 1910451
Source DB: PubMed Journal: Biofactors ISSN： 0951-6433 Impact factor: 6.113