Kean E A, Morrison E Y
Biochim Biophys Acta. 1979 Mar 16;567(1):12-7. doi: 10.1016/0005-2744(79)90166-9.
An enzyme which catalyses oxidative decarboxylation of branched-chain alpha-keto acids was extracted from rat liver mitochondria with the aid of NaClO4. Purification yielded a product which appeared homogenous upon electrophoresis. Some kinetic data are reported; however, the enzyme is inactive with alpha-ketoisovalerate. The tenacity of binding to mitochondria, specificity, and other features, suggest that the decarboxylase may be a component of an enzyme complex named alpha-ketoisocaproate: alpha-keto-beta-methylvalerate dehydrogenase.
借助高氯酸钠从大鼠肝脏线粒体中提取了一种催化支链α-酮酸氧化脱羧的酶。纯化后得到的产物在电泳时呈均一状态。报告了一些动力学数据;然而,该酶对α-酮异戊酸无活性。其与线粒体结合的牢固性、特异性及其他特性表明,该脱羧酶可能是名为α-酮异己酸:α-酮-β-甲基戊酸脱氢酶的酶复合物的一个组分。