人胎盘蛋白激酶C的分离与鉴定

Isolation and characterization of protein kinase C from human placenta.

作者信息

Tertrin-Clary C, Chenut M C, de la Llosa P

机构信息

Laboratoire des Hormones Polypeptidiques, CNRS, Gifsur-Yvette Cedex, France.

出版信息

Placenta. 1990 Jan-Feb;11(1):27-33. doi: 10.1016/s0143-4004(05)80440-0.

DOI:10.1016/s0143-4004(05)80440-0

PMID:2158087

Abstract

Protein kinase C (Ca2+ and phospholipid-dependent protein kinase) was detected in human placenta and was partially purified using DEAE cellulose chromatography and Ultrogel filtration. Diolein alone did not act on this enzyme but exerted a strong stimulatory action when associated with phosphatidylserine and Ca2+. Similar results were obtained with the phorbol myristate acetate. The kinetic constants for ATP, histone HI or Mg2+ and the apparent Ka for Ca2+ and phosphatidylserine were determined.

摘要

蛋白激酶C（钙和磷脂依赖性蛋白激酶）在人胎盘中被检测到，并通过二乙氨基乙基纤维素色谱法和优特胶过滤进行了部分纯化。仅二油精对该酶无作用，但与磷脂酰丝氨酸和钙离子结合时会产生强烈的刺激作用。佛波醇肉豆蔻酸酯乙酸盐也得到了类似的结果。测定了该酶对三磷酸腺苷、组蛋白H1或镁离子的动力学常数，以及对钙离子和磷脂酰丝氨酸的表观解离常数。