A Thrombin-Sensitive Protein of Human Platelet Membranes

  • Nancy Lewis Baenziger
    Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110
  • G. N. Brodie
    Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110
  • Philip W. Majerus
    Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

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<jats:p>The action of thrombin on intact human platelets has been studied with the aid of polyacrylamide gel electrophoresis in sodium dodecylsulfate. A single major membrane protein band with a molecular weight of 190,000 disappears after thrombin treatment, while a new membrane protein with a molecular weight of 107,000 appears. This may represent hydrolysis of the thrombin-sensitive protein. When platelets are disrupted or when the thrombin-sensitive protein is solubilized from membranes prior to thrombin treatment, no hydrolysis occurs. The effect of thrombin on the platelet membrane protein is complete within 2 min which suggests that hydrolysis of this membrane protein may trigger the physiological effects of thrombin on platelets.</jats:p>

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