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Platelet membrane glycoproteins IIb and IIIa were isolated and purified from human platelet membranes using lentil lectin affinity chromatography and electrophoretic elution from SDS-poly-acrylamide gels. Two dimensional immunoelectrophoresis of a mixture of the purified proteins against monospecific antisera showed antigenic uniqueness of the separate polypeptides. Computerized analysis of autoradiographs of two dimensional tryptic 125I peptide maps revealed that the two glycoproteins had completely different structures. Thus human platelet membrane glycoproteins IIb and IIIa are separate molecular entities. Monospecific anti-GPIIb and anti-GPIIIa were utilized in an enzyme linked immunosorbent assay system to demonstrate complex formation of the platelet glycoproteins with purified human fibrinogen. The formation of this GPIIb-GPIIIa fibrinogen complex is calcium dependent, fibrinogen specific, saturable, and inhibited by specific amino sugars and amino acids. These observations suggest that the GPIIb-GPIIIa macromolecular complex on the platelet surface acts under the proper physiologic circumstances as the fibrinogen binding site required for normal platelet aggregation.

Complex Formation Of Platelet Glycoproteins IIB And IIIA With Fibrinogen