Release of GPI-anchored Zn2+-glycerophosphocholine cholinephosphodiesterase as an amphiphilic form from bovine brain membranes by bee venom phospholipase A2.

摘要: Enzymatic release of Zn(2+)-glycerophosphocholine (GPC)cholinephosphodiesterase, as an amphiphilic form, from bovine brain membranes was examined. Of various membrane hydrolases, bee PLA2 the most effective in GPC cholinephosphodiesterase (amphiphilic 63-70%) membrane. Compared to pancreatic PLA2, more efficient cholinephosphodiesterase. In pH-dependent GP1-anchored phosphodiesterase, there a similar pH-release profile between PLA2-mediated and spontaneous one, implying involvement disruption action. The showed limited time-dependence (until 45 min) dose dependence (up 3 units/ml), characteristic receptor-type binding. An ionic binding may be alluded interfering effect anionic phospholipids on support interaction glycoproteins, action found blocked by lectins, wheat germ agglutinin or concanavalin A. combination with detergent, enhanced synergistically saponin, cholesterol-complexing agent. Meanwhile, additive lysolecithin suggests that is independent lysolecithin. It suggested specific sites membranes, probably rich GPI-anchored related facilitated proteins form.