TYROSINE PHOSPHORYLATION OF CYTOSOLIC PROTEINS IN HUMAN ERYTHROCYTES

被引：7

作者：

CLARI, G

LIBERA, LD

MORET, V

机构：

[1] CNR,CTR BIOMEMBRANE,I-35100 PADUA,ITALY

[2] UNIV PADUA,IST PATOL GEN,I-35100 PADUA,ITALY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 03期

关键词：

D O I：

10.1016/0006-291X(90)91019-O

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：

Some cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogenous Tyr-protein kinase(s). Their phosphorylation is enhanced by addition of Tyr-protein kinase, purified from human erythrocyte cytosol. The most phosphorylatable is a 19 kDa protein. Its phosphorylation is more activated by Mn2+ than by Mg2+. It is inhibited by NaCl, 2,3-bisphosphoglycerate and by heparin. Similar response to the above effectors is exhibited by the phosphorylation of the other protein bands. However, the phosphorylation of a 73 kDa double band, which is negligible in the absence of added NaCl, is stimulated by this salt. © 1990.

引用

页码：1378 / 1383

页数：6

共 26 条

[1] INTERACTIONS OF THE HUMAN RED-CELL MEMBRANE TYROSINE KINASE WITH HEPARIN [J].