从大鼠肝脏中纯化支链α-酮酸脱氢酶复合体
Purification of branched chain alpha-ketoacid dehydrogenase complex from rat liver.
作者信息
Shimomura Y, Paxton R, Ozawa T, Harris R A
出版信息
Anal Biochem. 1987 May 15;163(1):74-8. doi: 10.1016/0003-2697(87)90094-7.
PMID:3619032
Abstract
A new method using hydrophobic interaction chromatography on phenyl-Sepharose was developed to purify branched chain alpha-ketoacid dehydrogenase complex from commercially available frozen rat liver. Yields of greater than 50% were routinely achieved. The purified enzyme, composed of E1 alpha, E1 beta, and E2 subunits, appeared homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contained endogenous kinase activity for phosphorylation and inactivation of the complex.
摘要
开发了一种利用苯基琼脂糖凝胶上的疏水相互作用色谱法从市售冷冻大鼠肝脏中纯化支链α-酮酸脱氢酶复合体的新方法。常规产量大于50%。纯化后的酶由E1α、E1β和E2亚基组成，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上呈现均一性，并且含有使该复合体磷酸化和失活的内源性激酶活性。
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