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J. Biochem, 1988, Vol. 104, No. 4 628-632
© 1988 Japanese Biochemical Society


research-article

Functionally Active Thrombomodulin Is Present in Human Platelets1

Koji Suzuki1, Junji Nishioka, Tatsuya Hayashi and Yoshitane Kosaka

Department of Laboratory Medicine, Mie University School of Medicine Tsu, Mie 514

2To whom correspondence should be addressed

We found functionally active thrombomodulin in human platelets (60±18 molecules per platelet). Protein C appeared not to be activated by thrombin with gel-filtered platelets. However, the activation of protein C by thrombin was accelerated by thrombin-stimulated and washed platelets. This cofactor activity of the platelets was neutralized by the anti-lung thrombomodulin-F(ab')2 From the Triton X-extract of platelets, thrombomodulin was partially purified by diisopropylphosphoryl-thrombin-agarose affinity chromatography. The Mr of the predominant platelet thrombomodulin was 78,000 before and 109,000 after reduction on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, values identical to those of placental thrombomodulin. The specific activity of the cofactor activity, apparent Kd (0.4 nM) for thrombin and Km (0.67 µM) for protein C of platelet throm bomodulin were also identical to those of placenta thrombomodulin. Thrombomodulin may play a role in activation of protein C on the surface of platelets.

1This work was supported in part by Grants-in.Aid for Scientific Research (61571110, 62480433, and 63637001) from the Ministry of Education, Science and Culture of Japan.


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