P56LCK STABLY ASSOCIATES WITH A 115 KDA SUBSTRATE

被引：1

作者：

SRINIVAS, PR ^{[1
]}

HUTCHCORFT, JE ^{[1
]}

AUBE, BD ^{[1
]}

HARRISON, ML ^{[1
]}

机构：

[1] PURDUE UNIV, DEPT MEDICINAL CHEM & PHARMACOGNOSY, W LAFAYETTE, IN 47907 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 186卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80841-1

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：

Using antibodies directed against p561ck, we have identified a 115 kDa protein (p115) that is specifically immunoprecipitated with p561ck from whole cell lysates. The p561ck/p115 complex is stable in the presence of nonionic detergents. p115 becomes phosphorylated on tyrosine residues in p561ck immune-complex kinase assays. Treatment of whole cells with 12-O-tetradecanoyl phorbol-13-acetate decreases the subsequent tyrosine phosphorylation of p115 in immune-complex kinase assays. © 1992 Academic Press, Inc.

引用

页码：537 / 542

页数：6

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