Abstract
A 90-kDa protein-actin stable complex was purified from blood platelets by a short and efficient procedure giving at the same time actin used in polymerization assays. 90-kDa protein free of actin was prepared from the complex by 8 M ureau treatment and renaturation. By its molecular mass, immunological cross-reactivity with macrophage gelsolin and its effect on G- and F-actin the 90-kDa protein appears as the platelet gelsolin.
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