Aim A method has been developed for the rapid isolation of platelet membrane glycoproteins (GP) Ⅱ_b and Ⅲ_a. Methods The GP Ⅱ_b/Ⅲ_a complex was purified with concanavalin A-sepharose, heparin-sepharose and sephacryl S-300HR chromatography. Results The GP Ⅱ_b/Ⅲ_a complex, GP Ⅱ_b is composed of two disulfide-linked chains, a heavy chain of 125 kDa, called GPⅡ_bα, and a light chain of 23 kDa, called GP Ⅱ_bβ, in reduced conditions. The GP Ⅲ_a is a single polypeptide of 108 kDa in reduced conditions, or 95 kDa in nonreduced conditions. Conclusions Concanavalin A affinity chromatography was used to purify a platelet glycoprotein fraction. The concanavalin A-retained glycoproteins were eluted and adsorbed with a heparin-sepharose column to remove a major contaminant, thrombospondin. Sephacryl S-300 gel filtration was used as the final purification step to remove most fibrinogen and low-molecular-weight contaminants. The GP Ⅱ_b/Ⅲ_a complex can be used for the development of its biological products and further study.