牛肾支链α-酮酸脱氢酶激酶的纯化及性质
Purification and properties of branched-chain alpha-keto acid dehydrogenase kinase from bovine kidney.
作者信息
Lee H Y, Hall T B, Kee S M, Tung H Y, Reed L J
机构信息
Clayton Foundation Biochemical Institute, Austin, TX.
出版信息
Biofactors. 1991 Jun;3(2):109-12.
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.
支链α-酮酸脱氢酶（BCKDH）激酶从牛肾线粒体提取物中纯化了5000倍，达到明显的均一性。该激酶与BCKDH复合体共同纯化。用1.5 M NaCl和0.1% 2-巯基乙醇在pH 7.4条件下处理该复合体，然后通过Sephacryl S-400层析，约70%的激酶被释放出来。未结合的激酶通过Q Sepharose和Superose 12层析进一步纯化。纯化后的激酶是一种表观分子量约为43,000的单体。BCKDH激酶对丙酮酸脱氢酶几乎没有活性（如果有活性的话也极低）。
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