佛波酯受体与蛋白激酶C共纯化。
Phorbol diester receptor copurifies with protein kinase C.
作者信息
Niedel J E, Kuhn L J, Vandenbark G R
出版信息
Proc Natl Acad Sci U S A. 1983 Jan;80(1):36-40. doi: 10.1073/pnas.80.1.36.
Abstract
The phorbol diester receptor present in the particulate fraction of rat brain was solubilized by divalent ion chelation in the absence of detergents. The soluble receptor was partially purified by (NH4)2SO4 precipitation, DEAE-cellulose, and gel filtration chromatography. The purified receptor required exogenous phospholipid for activity and displayed a Kd of 7 nM for [3H]phorbol 12, 13-dibutyrate. Biologically active phorbol analogs inhibited binding, whereas inactive analogs did not. The Ca2+-dependent, phospholipid-sensitive protein kinase C copurified with the phorbol receptor. Purified protein kinase C was activated directly by phorbol 12-myristate 13-acetate in the presence of phospholipid.
摘要
大鼠脑微粒体部分存在的佛波酯受体在无去污剂的情况下通过二价离子螯合作用溶解。可溶性受体通过硫酸铵沉淀、DEAE-纤维素和凝胶过滤色谱法进行部分纯化。纯化后的受体需要外源性磷脂才能发挥活性，对[3H]佛波醇12,13-二丁酸酯的Kd为7 nM。具有生物活性的佛波醇类似物可抑制结合，而无活性的类似物则不能。钙离子依赖性、磷脂敏感的蛋白激酶C与佛波醇受体共同纯化。纯化后的蛋白激酶C在磷脂存在的情况下可被佛波醇12-肉豆蔻酸酯13-乙酸酯直接激活。
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