A 90 000-dalton actin-binding protein from platelets comparison with villin and plasma brevin
1982
Abstract Affinity chromatography of Ca 2+ -containing extracts of platelets on DNAase I-Sepharose, using Ca 2+ -free buffer as eluant, selects a 1:1 complex of a 90 000-dalton protein with actin. The complex shows little interaction with either DNAase or actin unless Ca 2+ is present. In the presence of Ca 2+ , the complex nucleates polymerization of actin, reduces the viscosity attained, and delays filament formation from profilactin with characteristics closely resembling those shown by chicken villin. Proteolysis of the native proteins indicates structural similarity between the platelet protein and villin or villin core; limited proteolytic digestion in the presence of SDS distinguishes the platelet protein from villin but not from the functionally related plasma protein, brevin. The platelet protein is not accessible to enzyme-mediated iodination of surface components on intact cells. The term ‘platelet brevin’ is proposed for the protein.
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