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• W2023896118 abstract "Calmodulin copurifies with platelet plasma membranes isolated by glycerol-induced lysis and density gradient centrifugation. These membranes also bind 125I-labeled calmodulin in vitro in the presence of Ca2+. Binding is largely reduced by replacing Ca2+ by Mg2+ or by addition of an excess unlabeled calmodulin. The specific component of binding is saturable, with an apparent Kd of 27 nM and a maximum of 15.9 pmol binding sites per mg of membrane protein. This is equivalent to approx. 4100 binding sites per platelet. Binding was inhibited by addition of phenothiazines, a group of calmodulin antagonists. Half-maximal inhibition was attained with approx. 20 μM trifluoperazine or 50 μM chlorpromazine. In contrast, chlorpromazine-sulfoxide which is inactive towards calmodulin, did not affect the binding. Calmodulin binding polypeptides of the plasma membrane were identified by a gel-overlay technique. A major calmodulin-binding component of molecular weight 149 000 was detected. Binding to this band was Ca2+-dependent and inhibited by chlorpromazine. The molecular weight of this polypeptide is similar to that of glycoprotein I and also that of the red cell (Ca2+ + Mg2+)-stimulated ATPase, which is known to bind calmodulin. The possible role of calmodulin in platelet activation is analysed." @default.
• W2023896118 created "2016-06-24" @default.
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• W2023896118 date "1982-03-01" @default.
• W2023896118 modified "2023-10-16" @default.
• W2023896118 title "Calmodulin binding to platelet plasma membranes" @default.
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• W2023896118 doi "https://doi.org/10.1016/0005-2736(82)90151-1" @default.
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