LIGHT-DEPENDENT PHOSPHORYLATION OF THYLAKOID MEMBRANE POLYPEPTIDES

被引：22

作者：

BELIVEAU, R ^{[1
]}

BELLEMARE, G ^{[1
]}

机构：

[1] UNIV LAVAL,FAC SCI & GENIE,DEPT BIOCHIM,QUEBEC CITY G1K 7P4,QUEBEC,CANADA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 88卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91478-5

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：

The phosphorylation of thylakoid membrane proteins was studied using isolated chloroplasts from Euglena gracilis. We have found, using [32P] labelling, that this phenomenon was light-driven, reversible in the dark, and completely inhibited by Carbonyl cyanide m-chlorophenyl-hydrazone (CCCP). Polyacrylamide gel electrophoresis containing SDS has revealed five main bands which have been found to be proteins. Amino acid analysis of the bands has shown that [32P] is incorporated into phosphothreonine. © 1979.

引用

页码：797 / 803

页数：7

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