Jones B S, Yeaman S J
Department of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, U.K.
Biochem J. 1991 May 1;275 ( Pt 3)(Pt 3):781-4. doi: 10.1042/bj2750781.
The kinase-activator protein (KAP) of pyruvate dehydrogenase complex (PDC) has been purified approx. 2250-fold from high-speed supernatants of mitochondrial extracts from the liver of 48 h-starved rats. Purified KAP demonstrates kinase activity towards both the E1 component of PDC and towards a synthetic peptide corresponding to the major phosphorylation site on E1. Furthermore, the activities of KAP and PDC kinase co-fractionate through several stages of purification and have the same apparent mass. We conclude that KAP is not a distinct protein, but is kinase which has dissociated from the complex.
丙酮酸脱氢酶复合体（PDC）的激酶激活蛋白（KAP）已从饥饿48小时大鼠肝脏线粒体提取物的高速上清液中纯化出来，纯化倍数约为2250倍。纯化后的KAP对PDC的E1组分以及与E1上主要磷酸化位点对应的合成肽均表现出激酶活性。此外，在几个纯化阶段中，KAP和PDC激酶的活性共同分级分离，且具有相同的表观质量。我们得出结论，KAP不是一种独特的蛋白质，而是从复合体中解离出来的激酶。
