title: Modulation of actin polymerization by 47,000-dalton protein of human platelets.
abstract: We purified 47,000-dalton proteins from both thrombin-stimulated and unstimulated human platelets. The purity of the protein was almost 80% on SDS-polyacrylamide gel electrophoresis. The protein obtained from unstimulated platelets strongly inhibited actin gelation when its molar ratio to actin was 1:200 or higher. The protein obtained from thrombin-stimulated platelets had no inhibitory activity. The results suggest that the 47,000-dalton protein modulates actin polymerization through phosphorylation.
authors.affiliation: Second Department of Biochemistry, Osaka City University Medical School, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Hashimoto
authors.forename: K
authors.initials: K
authors.lastname: Hashimoto
authors.forename: T
authors.initials: T
authors.lastname: Im
authors.forename: N
authors.initials: N
authors.lastname: Tatsumi
authors.forename: K
authors.initials: K
authors.lastname: Okuda
authors.forename: M
authors.initials: M
authors.lastname: Yukioka
mesh_terms: D000199:Actins / Q000097:blood*; D001792:Blood Platelets / Q000032:analysis*; D001798:Blood Proteins / Q000494:pharmacology*; D006801:Humans; D010750:Phosphoproteins; D010766:Phosphorylation; D011108:Polymers / Q000097:blood
chemical_list: D000199:Actins; D001798:Blood Proteins; D010750:Phosphoproteins; D011108:Polymers; C039077:platelet protein P47