Sulakhe P V, St Louis P J
Recent Adv Stud Cardiac Struct Metab. 1976;11:241-7.
Properties of the ATP-dependent calcium transport system of heart sarcolemma are presented. Calcium accumulation (with oxalate) in sarcolemma was increased due to cAMP-dependent protein kinase and phosphorylase b kinase. Protein kinase increased the Vmax of the sarcolemmal calcium accumulation without any detectable effect on the affinity for Ca2+. Both kinases failed to stimulate calcium binding. Protein kinase catalyzed phosphorylation of membrane proteins of molecular weights of 100,000, 25,000, and 14,000. Phosphorylase b kinase also catalyzed phosphorylation of these proteins. Protein kinase stimulated ATPase activity of sarcolemma. Sarcolemma contained endogenous protein kinase and protein phosphatase activities.
本文介绍了心脏肌膜ATP依赖钙转运系统的特性。由于cAMP依赖蛋白激酶和磷酸化酶b激酶的作用,肌膜中(与草酸盐结合的)钙积累增加。蛋白激酶增加了肌膜钙积累的Vmax,而对Ca2+亲和力没有任何可检测到的影响。两种激酶均未能刺激钙结合。蛋白激酶催化分子量为100,000、25,000和14,000的膜蛋白磷酸化。磷酸化酶b激酶也催化这些蛋白的磷酸化。蛋白激酶刺激了肌膜的ATP酶活性。肌膜含有内源性蛋白激酶和蛋白磷酸酶活性。