Abstract
Fibrinogen-binding platelet proteins have been examined by crossed-immunoelectrophoresis of solubilized, washed platelets followed by the incubation of the immunoplates with /sup 125/I-fibrinogen and exposure to x-ray films. Incubation with 0.1 mg/ml of /sup 125/I-fibrinogen revealed the binding of fibrinogen to the immunoprecipitates representing the glycoprotein IIb-IIIa complex, factor XIIIa chain, a granule membrane protein termed G4, fibrinogen, and albumin. Only the glycoprotein IIb-IIIa precipitate and the fibrinogen precipitate showed significant binding when the concentration of /sup 125/I-fibrinogen was lowered to 0.01 mg/ml. Thi indicates that the binding of fibrinogen is specific. The binding of /sup 125/I-fibrinogen to the precipitates representing the glycoprotein IIb-IIIa complex, the factor XIIIa chain, and G4, but not to the albumin precipitate, was significantly lowered in the presence of EDTA. This effect of EDTA increased with increasing pH, with no binding at pH 8.7. The results indicate that the glycoprotein IIb-IIIa complex, but not the separate glycoproteins IIb and IIIa, can act as Ca/sup 2 +/ or Mg/sup 2 +/-dependent fibrinogen receptor, under proper physiologic conditions.
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
