Activation of the branched-chain alpha-ketoacid dehydrogenase complex by a broad specificity protein phosphatase.
Activation of the branched-chain alpha-ketoacid dehydrogenase complex by a broad specificity protein phosphatase.
复制标题
广泛特异性蛋白磷酸酶激活支链 α-酮酸脱氢酶复合物。
DOI：
10.1016/s0006-291x(82)80168-x
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发表时间：
1982
影响因子：
3.1
通讯作者：
Parker,RA
中科院分区：
文献类型：
--
作者：
Harris,RA;Paxton,R;Parker,RA
从大鼠肝脏中纯化出一种广谱特异性蛋白磷酸酶，可激活粗组织提取物的磷酸化（无活性）支链α-酮酸脱氢酶复合物。这可以估计在不同生理状态下给定组织中活性（未磷酸化）复合物的比例。几乎所有（95%）的复合物都以活性形式存在于以亮氨酸作为唯一可氧化底物灌注的大鼠心脏中。相比之下，当灌注培养基中添加葡萄糖和胰岛素时，只有13%的复合物以活性形式存在。这些发现与先前在灌注大鼠心脏中通过复合物测量的通量率一致。
A broad-specificity protein phosphatase, purified from rat liver, can be used to activate the phosphorylated (inactive) branched-chain α-ketoacid dehydrogenase complex of crude tissue extracts. This enables estimation of the proportion of active (unphosphorylated) complex in a given tissue under different physiological states. Practically all (95 percent) of the complex was found in the active form in rat hearts perfused with leucine as the only oxidizable substrate. In contrast, only 13 percent of the complex was found in the active form when the perfusion medium was supplemented with glucose plus insulin. These findings are consistent with previously measured flux rates through the complex in perfused rat hearts.