Isolation, purification, and partial characterization of platelet membrane glycoproteins IIb and IIIa.
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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 sodium dodecyl sulfate-polyacrylamide 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. Monospecific anti-glycoproteins IIb and IIIa Fab'2 fragments, either singly or in combination, induced platelet agglutination but did not inhibit or alter the platelet aggregation response to physiologic stimuli. The results demonstrate that human platelet membrane glycoproteins IIb and IIIa are separate molecular entities. In the native state, the membrane macromolecular IIb.IIIa complex may play an important role in mediating platelet-platelet interactions.
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