钙调蛋白与磷脂酶A2亚基的钙依赖性结合诱导酶促激活。

Calcium-dependent binding of calmodulin to phospholipase A2 subunits induces enzymatic activation.

作者信息

Moskowitz N, Andrés A, Silva W, Shapiro L, Schook W, Puszkin S

出版信息

Arch Biochem Biophys. 1985 Sep;241(2):413-7. doi: 10.1016/0003-9861(85)90564-8.

Abstract

Calmodulin interacted with phospholipase A2 from two different sources, as established by affinity chromatography, dimethylsuberimidate protein crosslinking, and phospholipase A2 assays. Calmodulin was covalently crosslinked to pancreatic and bee venom phospholipases A2 in a calcium-dependent manner, and enhanced the enzymatic activities of these phospholipases. Pancreatic phospholipase A2 was separated into two species of identical molecular weight by calmodulin affinity chromatography; the species that bound to immobilized calmodulin in a calcium-dependent manner was stimulated by calmodulin. This presents further evidence that phospholipase A2 is directly activated by calmodulin.

摘要

通过亲和色谱法、亚胺二甲酯蛋白质交联法和磷脂酶A2测定法证实，钙调蛋白与来自两种不同来源的磷脂酶A2相互作用。钙调蛋白以钙依赖的方式与胰腺和蜂毒磷脂酶A2共价交联，并增强了这些磷脂酶的酶活性。通过钙调蛋白亲和色谱法将胰腺磷脂酶A2分离成两种分子量相同的物质；以钙依赖方式与固定化钙调蛋白结合的物质受到钙调蛋白的刺激。这进一步证明磷脂酶A2是由钙调蛋白直接激活的。