Abstract
Membrane proteins of both control and thrombin-treated human platelets were labeled by ( 3H)-sodium borohydride reduction of Schiff bases formed between pyridoxal phosphate and protein amino groups. Fluorographic analysis of solubilized platelet proteins disclosed a substantial difference between the labeling patterns of control vs. thrombin-treated cells. Whereas the normal platelets showed a single intensely labeled protein band, cells exposed to thrombin showed about ten labeled polypeptides. When thrombin-induced serotonin release from platelets was blocked by 3′,5′-adenosine diphosphate, the protein labeling pattern on the fluorograph resembled that of control platelets. These data suggest that serotonin release from platelets by thrombin involve major changes in the architecture of proteins of platelets surface.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
