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We have developed hybridoma cell lines that produce monoclonal antibodies directed to different components on the human platelet membrane. One of these lines produces an antibody, named Tab, that binds to a protein on normal platelets that is deficient in platelets from patients with Glanzmann’s thrombasthenia. We isolated this protein from Triton X-100 solubilized normal platelet membranes by affinity chromatography on Tab-agarose. As determined by SDS polyacrylamide gel electrophoresis, the isolated protein consists of two polypeptides previously designated as glycoproteins IIb and IIIa. The isolation of two polypeptides by a single monoclonal antibody suggests that IIb and IIIa are subunits of a single molecule. We prepared 125I-Tab to determine the number of glycoprotein IIb-IIIa molecules on normal and thrombasthenic platelets by a direct binding assay. Platelets from 17 normal individuals bound 39,000 ± 4,600 Tab molecules/platelet. Platelets from four patients with thrombasthenia lacked Tab binding sites (&lt;5%) . Nine heterozygotes for thrombasthenia bound 24,500 ± 5,800 Tab molecules/platelet. We separated the IIb and IIIa subunits by preparative gel electrophoresis and analyzed their structures. Both polypeptides contain ∼15% carbohydrate, but IIIa has a higher percentage of mannose residues. The amino acid compositions are similar, suggesting some sequence homology. However, tryptic peptide maps of 125I IIb and 131I IIIa, analyzed simultaneously by high performance liquid chromatography, are completely different. This indicates that neither subunit is derived from the other and suggests that IIb and IIIa may be products of separate genes. The Tab antibody should prove useful in further elucidation of the structure and function of glycoprotein IIb-IIIa. Other monoclonal antibodies may serve as valuable probes of additional platelet membrane proteins.

Isolation And Characterization Of Platelet Membrane Glycoprotein IIB-IIIa With A Monoclonal Antibody