Factor Va-dependent binding of factor Xa to human platelets.
نویسندگان
چکیده
منابع مشابه
Properties of the factor Xa binding site on human platelets.
The affinity (Ka) of human coagulation Factor Xa for thrombin-treated (to stimulate the release reaction) platelets has been determined to be 3 to 4 x 10(10) M-1 by equilibrium binding studies using 125I-labeled Xa. The binding of Factor Xa to platelets results in an increase of 300,000-fold in the apparent enzymatic activity of Xa in the conversion of prothrombin to thrombin. The activity of p...
متن کاملDeficiency of factor Xa-factor Va binding sites on the platelets of a patient with a bleeding disorder.
Factor V (Va) is essential for binding of factor Xa to the surface of platelets. After thrombin treatment, normal platelets release at least five times more factor Va activity than is required for maximal factor Xa binding. The concentration of factor V activity obtained after thrombin stimulation of 10(7) normal platelets is sufficient to allow half-maximal factor Xa binding to 10(8) platelets...
متن کاملCoordinate binding of factor Va and factor Xa to the unstimulated platelet.
The interaction of Factor Xa and Factor Va at the platelet surface was investigated by direct, simultaneous binding measurements of both proteins to platelets and by immunochemical and kinetic techniques. Binding measurements of 125I-Factor Xa and 131I-Factor Va to unstimulated platelets indicate that the amount of Factor Xa bound is proportional to the amount of Factor Va bound. At saturating ...
متن کاملInteraction of coagulation factor Xa with human platelets.
When human 125I-labeled Factor Xa is incubated with washed platelets, prothrombin, and Ca2+, a small amount of thrombin is formed which causes the platelet release reaction after a period of time that decreases as the Xa concentration is increased from 0.9 to 19 ng/ml. After a further lag period, the Xa binds reversibly to receptors on the platelet surface and rapid thrombin formation follows (...
متن کاملDefective binding of factor XI-N248 to activated human platelets.
Variants of factor XI containing Gln226 to Arg (Q226 to R) and Ser248 to Asn (S248 to N) substitutions were first identified in an African American family with a history of excessive bleeding. The substitutions have recently been identified in unrelated individuals, suggesting they are relatively common. Both amino acids are located in the third apple domain of factor XI, an area implicated in ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)86158-6