Liu L X, Nardi M A, Flug F, Karpatkin S
Department of Medicine, New York University Medical Center, N.Y. 10016.
Thromb Res. 1992 May 15;66(4):309-20. doi: 10.1016/0049-3848(92)90281-e.
A unique murine monoclonal antibody (LK-4) is described which differentiates PLA1/PLA1 platelet extracts from PLA2/PLA2 and PLA1/PLA2 platelet extracts on solid phase ELISA and immunoblot at the 100kD GPIIIa location, but not on intact platelets. LK-4 reacts equally with intact PLA1/PLA2 and PLA2/PLA2 platelets. Adsorbtion of LK-4 with PLA1/PLA1 platelets results in loss of reactivity for intact platelets as well as platelet extracts on ELISA or immunoblot. LK-4 inhibits platelet aggregation induced by ADP, epinephrine, collagen and thrombin, suggesting reactivity at or near the fibrinogen binding site on GPIIIa. It is suggested the LK-4 reacts with a conformation-induced common epitope for PLA1 and PLA2 on GPIIIa, with loss of this conformation for PLA2 GPIIIa following solubilization with Triton X-100.
描述了一种独特的鼠单克隆抗体（LK - 4），该抗体在固相酶联免疫吸附测定（ELISA）和免疫印迹中，能在100kD糖蛋白IIIa（GPIIIa）位置区分PLA1/PLA1血小板提取物与PLA2/PLA2和PLA1/PLA2血小板提取物，但在完整血小板上则不能区分。LK - 4与完整的PLA1/PLA2和PLA2/PLA2血小板具有同等反应性。用PLA1/PLA1血小板吸附LK - 4会导致其对完整血小板以及ELISA或免疫印迹中的血小板提取物失去反应性。LK - 4抑制由二磷酸腺苷（ADP）、肾上腺素、胶原蛋白和凝血酶诱导的血小板聚集，提示其在GPIIIa上纤维蛋白原结合位点处或附近具有反应性。有人提出LK - 4与GPIIIa上PLA1和PLA2的构象诱导共同表位发生反应，在用 Triton X - 100溶解后，PLA2 GPIIIa的这种构象会丧失。
