McMurray W C, Irvine R F
Department of Biochemistry, Institute of Animal Physiology and Genetics Research, Babraham, Cambridge, U.K.
Biochem J. 1988 Feb 1;249(3):877-81. doi: 10.1042/bj2490877.
A phospholipase C which hydrolyses phosphatidylinositol 4,5-bisphosphate to release inositol trisphosphate was detected in a sedimentable fraction from celery and from some other higher plants. The particulate enzyme also hydrolyses phosphatidylinositol, whereas the soluble phosphatidylinositol phosphodiesterase described previously [Irvine, Letcher & Dawson (1980) Biochem. J. 192, 279-283] acts only on phosphatidylinositol, and we were unable to detect activity of this soluble activity on phosphatidylinositol 4,5-bisphosphate. Activity of the particulate enzyme is markedly enhanced in the presence of deoxycholate, but not of other detergents; the particulate enzyme can also be solubilized by extraction with deoxycholate.
在芹菜及其他一些高等植物的可沉降组分中检测到一种磷脂酶C,它能水解磷脂酰肌醇4,5 - 二磷酸以释放肌醇三磷酸。这种颗粒性酶也能水解磷脂酰肌醇,而先前描述的可溶性磷脂酰肌醇磷酸二酯酶[欧文、莱彻和道森(1980年)《生物化学杂志》192, 279 - 283]仅作用于磷脂酰肌醇,并且我们未能检测到该可溶性活性对磷脂酰肌醇4,5 - 二磷酸的活性。在脱氧胆酸盐存在下,颗粒性酶的活性显著增强,但在其他去污剂存在下则不然;颗粒性酶也可用脱氧胆酸盐提取进行增溶。