ENHANCEMENT OF GTP-GAMMA S-BINDING ACTIVITY BY CAMP-DEPENDENT PHOSPHORYLATION OF A FILAMIN-LIKE 250-KDA MEMBRANE-PROTEIN IN HUMAN PLATELETS

被引：14

作者：

YADA, Y ^{[1
]}

OKANO, Y ^{[1
]}

NOZAWA, Y ^{[1
]}

机构：

[1] GIFU UNIV, SCH MED, DEPT BIOCHEM, TSUKASAMACHI 40, GIFU 500, JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 172卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80202-5

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 treatment of human platelets with the dibutyryl cyclic AMP (dbcAMP) revealed the presence of a 250 kDa protein which enhanced its GTP-binding activity. This protein was purified from platelet membranes by successive chromatographies on DEAE-cellulose, Ultrogel AcA34, Mono Q, HCAhydroxyapatite, and TSK-3000SW columns. The positive cross-reaction of the 250 kDa protein with the anti-filamin antibody indicated that this protein is filamin or very close to it. The GTP γS-binding activity of this protein, when phosphorylated with cyclic AMP-dependent protein kinase (A-kinase), showed an over tenfold increase, with the specific activity being 3.6 nmol/mg protein. Dephosphorylation of the phosphorylated protein with alkaline phosphatase reduced the GTP γ S-binding activity to the control untreated level. © 1990 Academic Press, Inc.

引用

页码：256 / 261

页数：6

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