IDENTIFICATION AND CHARACTERIZATION OF THE CAMP BINDING-PROTEINS OF YEAST BY PHOTOAFFINITY-LABELING

被引：13

作者：

DERY, C

COOPER, S

SAVAGEAU, MA

SCANLON, S

机构：

[1] Department of Microbiology, Immunology The University of Michigan, Ann Arbor

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 90卷 / 03期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0006-291X(79)91917-X

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：

Contrary to previous reports, we find the molecular weight of the major cAMP-binding protein in Saccharomyces cerevisiae to be 54,000 daltons. A number of lower molecular weight proteins have also been identified and are believed to be breakdown products of the major protein. The binding protein is soluble and specific for cyclic purine nucleotides with a 3′:5′ configuration. © 1979.

引用

页码：933 / 939

页数：7

共 13 条

[1]

COOPER SJ, UNPUBLISHED

[2]

FREIDMAN DL, 1978, P NAT ACAD SCI US, V75, P5286

[3] A PROTEIN BINDING ASSAY FOR ADENOSINE 3'-5'-CYCLIC MONOPHOSPHATE [J].