Purification and properties of the catalytic subunit of the branched-chain alpha-keto acid dehydrogenase phosphatase from bovine kidney mitochondria.
作者： Z. Damuni , L.J. Reed
DOI: 10.1016/S0021-9258(18)61164-0
关键词:
摘要: The catalytic subunit of the branched-chain alpha-keto acid dehydrogenase (BCKDH) phosphatase (Damuni, Z., Merryfield, M.L., Humphreys, J.S., and Reed, L.J., (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 4335-4338) has been purified over 50,000-fold from extracts bovine kidney mitochondria. apparently homogeneous protein consists a single polypeptide chain with an apparent Mr = approximately 33,000 as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. BCKDH phosphatase, 460,000, was dissociated to its no change in activity, at early stage purification procedure treatment 6 M urea. specific activity 1,500-2,500 units/mg. exhibited 10% maximal 32P-labeled pyruvate complex but inactive phosphorylase p-nitrophenyl phosphate. subunit, like 460,000 species, inhibited nanomolar concentrations inhibitor protein, unaffected 1 2, nucleoside tri- diphosphates not monophosphates.
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