PLASMIN DIGESTION OF HUMAN FIBRINOGEN PREVIOUSLY PHOSPHORYLATED BY PROTEIN KINASE-C OR DEPHOSPHORYLATED BY ALKALINE-PHOSPHATASE INVITRO

被引：16

作者：

FORSBERG, PO

MARTIN, SC

机构：

[1] Department of Medical and Physiological Chemistry, Biomedical Centre, University of Uppsala

来源：

THROMBOSIS RESEARCH | 1990年 / 58卷 / 02期

关键词：

fibrinogen; phosphorylation; plasmin; protein kinase C; streptokinase; tissue plasminogen activator; urokinase;

D O I：

10.1016/0049-3848(90)90169-D

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Human fibrinogen, either untreated or previously phosphorylated by protein kinase C, was incubated with plasmin generated by streptokinase, urokinase or tissue plasminogen activator and the resulting fragments were separated by gel electrophoresis. Plasmin degradation resulted in the expected X, Y and D fragments, but the degradation rates differed. In vitro phosphorylation of fibrinogen was seen to inhibit the plasmin digestion. Treatment with alkaline phosphatase did not reverse the inhibition. © 1990.

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页码：119 / 127

页数：9

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