从大鼠肝脏、肾脏和心脏分离出的线粒体中支链2-氧代酸脱氢酶复合体的多位点磷酸化作用。
Multi-site phosphorylation of branched-chain 2-oxoacid dehydrogenase complex within mitochondria isolated from rat liver, kidney and heart.
作者信息
Cook K G, Lawson R, Yeaman S J
出版信息
FEBS Lett. 1983 Nov 28;164(1):85-8. doi: 10.1016/0014-5793(83)80024-6.
PMID:6653787
Abstract
The alpha subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase complex becomes rapidly phosphorylated in rat liver, kidney and heart mitochondria incubated in the presence of succinate and [32P]phosphate. Peptide mapping of tryptic digests of the phosphorylated alpha subunit indicates that 3 distinct sites are phosphorylated, as has been reported previously by us for phosphorylation in vitro of highly purified complex.
摘要
在琥珀酸和[32P]磷酸盐存在的情况下孵育的大鼠肝脏、肾脏和心脏线粒体中，支链2-氧代酸脱氢酶复合体E1组分的α亚基会迅速发生磷酸化。对磷酸化α亚基的胰蛋白酶消化产物进行肽图谱分析表明，有3个不同的位点发生了磷酸化，这与我们之前报道的高度纯化复合体的体外磷酸化情况一致。
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