Savart M, Belamri M, Pallet V, Ducastaing A
FEBS Lett. 1987 May 25;216(1):22-6. doi: 10.1016/0014-5793(87)80749-4.
Calpains 1 and 2 co-eluted with protein kinase C activities after hydrophobic (phenyl-Sepharose) and anion-exchange (Mono Q) chromatographies of a 100,000 X g supernatant which was defined as cytosol. After centrifugation of the cytosol at 200,000 X g for 16 h, the major part of calpain 1 and of its associated protein kinase C activity was recovered in the pellet, when the major part of calpain 2, also associated to a protein kinase C activity, was present in the resulting supernatant. Polyacrylamide gel electrophoresis of the fractions eluted from the Mono Q column, which contained calpains 1 or 2 and their associated protein kinase C activities, revealed two main bands with a molecular mass of 80 and 28 kDa.
在对定义为胞质溶胶的100,000×g上清液进行疏水（苯基琼脂糖）和阴离子交换（Mono Q）色谱分析后，钙蛋白酶1和2与蛋白激酶C活性共同洗脱。将胞质溶胶在200,000×g下离心16小时后，钙蛋白酶1及其相关蛋白激酶C活性的大部分存在于沉淀中，而钙蛋白酶2的大部分（同样与蛋白激酶C活性相关）则存在于所得上清液中。对从Mono Q柱洗脱的含有钙蛋白酶1或2及其相关蛋白激酶C活性的级分进行聚丙烯酰胺凝胶电泳，显示出两条主要条带，分子量分别为80 kDa和28 kDa。
