A Thrombin-Sensitive Protein of Human Platelet Membranes

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 we...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1971-01, Vol.68 (1), p.240-243
Main Authors: Baenziger, Nancy Lewis, Brodie, G. N., Majerus, Philip W.
Format: Article
Language:English
Subjects:
Biological Sciences: Medical Sciences
Blood Platelets - drug effects
Blood Proteins - analysis
Cell membranes
Detergents
Diphosphates
Electrophoresis
Electrophoresis, Disc
Gels
Humans
Hydrolysis
Membrane proteins
Membranes - drug effects
Molecular Weight
P branes
Platelets
Sodium
Solubility
Sulfuric Acids
Thrombin - pharmacology
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.68.1.240