Nachman R L, Jaffe E A, Weksler B B
J Clin Invest. 1977 Jan;59(1):143-8. doi: 10.1172/JCI108612.
Human platelets washed and fixed in paraformaldehyde aggregate in the presence of the antibiotic ristocetin and normal plasma. This aggregation response is abolished after digestion of the fixed platelets with chymotrypsin. Antisera to fixed washed platelets were produced in rabbits and absorbed with chymotrypsin-treated, fixed washed platelets. Monovalent Fab fragments obtained from the isolated gamma-globulin fractions of the antisera blocked ristocetin-induced aggregation of fixed washed platelets in buffer and normal platelets in platelet-rich plasma. By double-antibody immunoprecipitation, it was shown that the antibody which blocked the ristocetin reaction interacted with a platelet membrane surface protein of mol wt 155,000. The results suggest that the glycoprotein I complex on the surface of the human platelet mediates ristocetin-induced von Willebrand factor-dependent platelet aggregation.
经洗涤并用多聚甲醛固定的人血小板,在抗生素瑞斯托霉素和正常血浆存在的情况下会发生聚集。在用胰凝乳蛋白酶消化固定后的血小板后,这种聚集反应消失。用固定洗涤后的血小板免疫家兔制备抗血清,并用经胰凝乳蛋白酶处理的固定洗涤血小板吸收该抗血清。从抗血清的分离γ-球蛋白组分获得的单价Fab片段,可阻断缓冲液中固定洗涤血小板以及富含血小板血浆中正常血小板的瑞斯托霉素诱导的聚集。通过双抗体免疫沉淀法表明,阻断瑞斯托霉素反应的抗体与分子量为155,000的血小板膜表面蛋白相互作用。结果表明,人血小板表面的糖蛋白I复合物介导瑞斯托霉素诱导的血管性血友病因子依赖性血小板聚集。