Modulation of actin polymerization by 47,000-dalton protein of human platelets.
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.
Hashimoto
K
K
Second Department of Biochemistry, Osaka City University Medical School, Japan.
Hashimoto
K
K
Im
T
T
Tatsumi
N
N
Okuda
K
K
Yukioka
M
M
D000199:Actins / Q000097:blood*; D001792:Blood Platelets / Q000032:analysis*; D001798:Blood Proteins / Q000494:pharmacology*; D006801:Humans; D010750:Phosphoproteins; D010766:Phosphorylation; D011108:Polymers / Q000097:blood
D000199:Actins; D001798:Blood Proteins; D010750:Phosphoproteins; D011108:Polymers; C039077:platelet protein P47