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- Nancy Lewis Baenziger
- Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110
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- G. N. Brodie
- Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110
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- Philip W. Majerus
- Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110
抄録
<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>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 68 (1), 240-243, 1971-01
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1362544421263432448
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- NII論文ID
- 30016258284
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- ISSN
- 10916490
- 00278424
- http://id.crossref.org/issn/00278424
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