Miller J J, Browne P C, Detwiler T C
Department of Biochemistry, State University of New York Health Science Center at Brooklyn 11203.
Biochem Biophys Res Commun. 1988 Feb 29;151(1):9-15. doi: 10.1016/0006-291x(88)90552-9.
A labeled 77-kDa complex formed when 125I-thrombin was added to platelet suspensions or to the supernatant solution of ionophore-activated platelets. Prostacyclin inhibited complex formation with whole platelets but not with the supernatant solution of ionophore-activated platelets. This is evidence that the complex formed with a factor secreted from activated platelets. Smaller complexes of 70 and 58 kDa formed between labeled thrombin and lysed platelets. The 77-kDa complex was necessary for the formation of a thrombin-thrombospondin complex.
当将¹²⁵I-凝血酶添加到血小板悬液或离子载体激活的血小板的上清液中时,会形成一种标记的77-kDa复合物。前列环素抑制与完整血小板形成复合物,但不抑制与离子载体激活的血小板的上清液形成复合物。这证明该复合物是由活化血小板分泌的一种因子形成的。标记的凝血酶与裂解的血小板之间形成了70 kDa和58 kDa的较小复合物。77-kDa复合物是凝血酶-血小板反应蛋白复合物形成所必需的。