PMID: 2106289Feb 1, 1990Paper

Characteristics of a thrombin inhibitor secreted by activated platelets

Archives of Biochemistry and Biophysics
J J Miller, T C Detwiler

Abstract

A 77-kDa complex of thrombin and a protein secreted by activated platelets had little if any thrombin amidolytic activity, indicating that the secreted protein is an inhibitor. The molecular weight of the inhibitor before reaction with thrombin was approximately 50,000. The apparent second-order rate constant for complex formation was estimated to be 1.3 x 10(6) M-1 s-1 (mean of four measurements); it was not affected by heparin or heparinase. These properties distinguish this inhibitor from other protease inhibitors secreted by platelets. The inhibitor reacted with trypsin and possibly with urokinase but not with factor Xa.

References

Aug 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·K M Lerea, J A Glomset
Feb 29, 1988·Biochemical and Biophysical Research Communications·J J MillerT C Detwiler
Jan 1, 1985·The Journal of Clinical Investigation·A H SchmaierR W Colman
Jan 1, 1984·Journal of Biochemistry·K SuzukiS Hashimoto
Oct 1, 1984·The Journal of Clinical Investigation·L A EricksonD J Loskutoff

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Citations

Sep 15, 1995·Thrombosis Research·K Chen, D W Essex
Jun 28, 1991·Biochemical and Biophysical Research Communications·A C Chang, T C Detwiler
Nov 15, 1992·Archives of Biochemistry and Biophysics·A C Chang, T C Detwiler

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