CALMODULIN BINDING AND PROTEIN-PHOSPHORYLATION IN ADRENAL-MEDULLA COATED VESICLES

被引：11

作者：

GEISOW, MJ

BURGOYNE, RD

机构：

[1] National Institute for Medical Research, The Ridgeway, London, NW7 1AA England, Mill Hill

来源：

FEBS LETTERS | 1984年 / 169卷 / 02期

关键词：

Adrenal medulla; Ca[!sup]2+[!/sup] calmodulin; Chromaffin cell; Clathrin; Coated vesicle; Phosphorylation;

D O I：

10.1016/0014-5793(84)80303-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Coated vesicles from bovine adrenal medulla contained clathrin and major detergent-insoluble polypeptides of 120-100, 51 and 49 kDa. Intact coated vesicles and vesicles lacking clathrin light chains were bound by immobilized calmodulin in the presence of Ca2+. Clathrin in the form of 700 Å cages was not bound. The calmodulin binding components in intact coated vesicles are therefore contributed by the enclosed vesicle or by the 120-100, 50 or 49 kda polypeptides. The 51 kDa component incorporated 32Pi from labelled ATP by an endogenous kinase activity; no other coat or vesicle membrane protein was phosphorylated in vitro, either by intrinsic or exogenous kinases. © 1984.

引用

页码：127 / 132

页数：6