Calcium-dependent binding of calmodulin to phospholipase A"2 subunits induces enzymatic activation - Moskowitz, N.; Andres, A.; Silva, W.; Shapiro, L.; Schook, W.; Puszkin, S. (Elsevier)
Calmodulin interacted with phospholipase A"2 from two different sources, as established by affinity chromatography, dimethylsuberimidate protein crosslinking, and phospholipase A"2 assays. Calmodulin was covalently crosslinked to pancreatic and bee venom phospholipases A"2 in a calcium-dependent manner, and enhanced the enzymatic activities of these phospholipases. Pancreatic phospholipase A"2 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 A"2 is directly activated by calmodulin.
http://dx.doi.org/10.1016/0003-9861(85)90564-8
Keywords: W; V; U