Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase.

Evidence that a 41,000 dalton brain phosphoprotein is pyruvate dehydrogenase.
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有证据表明 41,000 道尔顿的脑磷蛋白是丙酮酸脱氢酶。

DOI:
10.1016/0006-291x(80)90822-0
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发表时间:
1980
影响因子:
3.1
通讯作者:
Routtenberg,A
Routtenberg,A
中科院分区:
生物学4区
文献类型:
--
作者:
Morgan,DG;Routtenberg,A

文献摘要

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Phosphorylation of a brain protein of Mr=41,000, termed band F2, is selectively regulated by effectors of pyruvate dehydrogenase kinase (pyruvate, dichloroacetate, NAD, NADH, CoA, and acetyl CoA). Subcellular fractionation studies indicate a mitochondrial localization of a phosphoprotein with this molecular weight. The phosphorylated α-subunit of purified bovine kidney pyruvate dehydrogenase comigrates with band F2on polyacrylamide gels and both appear as a doublet band of Mr=41,000−42,000. On the basis of similar regulatory properties, subcellular location and electrophoretic mobility, we propose that band F2is the α-subunit of the brain pyruvate dehydrogenase complex. Because band F2can be affected by physiological and behavioral treatments, our hypothesis suggests a potential regulatory role for pyruvate dehydrogenase in brain function.