Laychock S G, Franson R C, Weglicki W B, Rubin R P
Biochem J. 1977 Jun 15;164(3):753-6. doi: 10.1042/bj1640753.
Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca2+ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca2+-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.
在胰蛋白酶分散的猫肾上腺皮质细胞的匀浆和亚细胞组分中测定了磷脂酶A活性。在pH 7.4时,匀浆中的磷脂水解被添加的Ca2+激活,并被EGTA抑制。在有和没有辛纳肽的情况下,磷脂降解都被EGTA完全阻断。膜结合磷脂酶的Ca2+依赖性激活可能是调节辛纳肽刺激过程中发生的分子变化的关键控制机制。