BIP IS A SUBSTRATE FOR SRC KINASE IN-VITRO

被引：10

作者：

CARLINO, A

TOLEDO, H

VIDAL, V

REDFIELD, B

STRASSMAN, J

ABDELGHANY, M

RACKER, E

WEISSBACH, H

BROT, N

机构：

[1] ROCHE INST MOLEC BIOL,ROCHE RES CTR,NUTLEY,NJ 07110

[2] CORNELL UNIV,DIV BIOL SCI,BIOCHEM MOLEC & CELL BIOL SECT,ITHACA,NY 14853

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 201卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.1880

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：

In a study to investigate the ability of chaperones to modulate src kinase activity, it was observed that BiP, a member of the HSP70 family found in the endoplasmic reticulum, is an excellent substrate for src kinase in vitro. The reaction requires polylysine and the results suggest that two tyrosine residues are phosphorylated. Although there is no evidence for this reaction invivo, it does provide a very efficient method to label BiP. (C) 1994 Academic Press, Inc.

引用

页码：1548 / 1553

页数：6

共 30 条

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