Purification and characterization of a calcium binding protein with "synexin-like" activity from human blood platelets.
A calcium binding protein of Mr = 54,000 has been isolated from human blood platelets. This protein has been shown to enhance Ca2+-induced aggregation of phosphatidylserine liposomes, suggesting that it may be a member of a recently recognized class of binding proteins known to interact with phospholipids and the membrane in a Ca2+ dependent manner. Because of the "synexin-like" activity of this protein it may be involved in Ca2+ regulated platelet secretion as well as cell motility.
Zhuang
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Department of Biochemistry, State University of New York Health Science Center at Brooklyn 11203.
Stracher
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D017310:Annexin A7; D001345:Autoradiography; D001792:Blood Platelets / Q000032:analysis*; D001798:Blood Proteins; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000097:blood*; D002848:Chromatography, DEAE-Cellulose; D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008081:Liposomes / Q000378:metabolism; D008970:Molecular Weight; D010718:Phosphatidylserines / Q000378:metabolism
D017310:Annexin A7; D001798:Blood Proteins; D002135:Calcium-Binding Proteins; D008081:Liposomes; D010718:Phosphatidylserines; D003101:Collodion; D002118:Calcium