Sankaran K, Pawse A R, Nadkarni G B
Biochim Biophys Acta. 1976 Jul 8;438(2):412-23. doi: 10.1016/0005-2744(76)90258-8.
The mitochondria of liver of Yoshida ascites tumour-bearing rats contained two forms of protein kinase distinguishable on the basis of their kinetic properties, substrate specificity and responses to cyclic adenosine 3',5'-monophosphate (cAMP). One of these (kinase I) was activated 2-3 fold by cAMP while the other form (kinase II) was insensitive to the action of cAMP. Kinase I which was selective towards histone F1 as substrate was obtained as a homogeneous preparation and was observed to have a molecular weight of 170 000 by Sephadex G-150 gel filtration. Protein kinase II appeared to be a smaller protein with molecular weight of 54 000 and was specific towards acidic proteins namely casein and phosvitin. Protein kinases isolated from liver mitochondria of normal rats showed variations in respect to elution profile of DEAE-cellulose and electrophoretic mobility. The preparation corresponding to kinase I did not show stimulatory responses to cAMP.
吉田腹水瘤大鼠肝脏的线粒体含有两种蛋白激酶，根据其动力学特性、底物特异性和对环磷酸腺苷（cAMP）的反应可加以区分。其中一种（激酶I）被cAMP激活2至3倍，而另一种形式（激酶II）对cAMP的作用不敏感。以组蛋白F1为底物具有选择性的激酶I是一种均一制剂，通过葡聚糖G - 150凝胶过滤观察到其分子量为170000。蛋白激酶II似乎是一种分子量为54000的较小蛋白质，对酸性蛋白质即酪蛋白和卵黄高磷蛋白具有特异性。从正常大鼠肝脏线粒体中分离出的蛋白激酶在DEAE - 纤维素洗脱图谱和电泳迁移率方面存在差异。与激酶I相对应的制剂对cAMP未表现出刺激反应。
