Peleg I, Eldor A, Muhlrad A, Groschel-Stewart U, Kahane I
Thromb Res. 1985 Jun 1;38(5):567-76. doi: 10.1016/0049-3848(85)90189-6.
Myosins were purified from the membrane fraction and the cytoplasm of human platelets. Polyclonal antibodies to the purified myosins were induced in rabbits. Their effects on the ATPase activity of the purified myosins as well as on the process of platelet aggregation were studied. A strong cross reactivity was found between the two myosins and their respective antibodies by the ELISA technique. It was found that the antibodies preferentially bind to the "head" segment of the myosins, since purified myosin "rod" reacted only weakly with the two kinds of antibodies. The two antimyosin antibodies strongly inhibited the K+(EDTA) ATPase activity of both myosins, as well as the activity of the isolated myosin "heads". The amount of antimembrane myosin antibody required to inhibit the above enzymatic activity was smaller than that of the anticytoplasmatic myosin antibody. Similar results were observed with F(ab)2 fragments of the two kinds of antibodies. No effect of these antibodies or their F(ab)2 fragments was observed on platelet aggregation induced by various agonists, although their inhibitory effect on the platelet myosin ATPase activity was strong.
从人血小板的膜部分和细胞质中纯化肌球蛋白。在兔体内诱导产生针对纯化肌球蛋白的多克隆抗体。研究了它们对纯化肌球蛋白的ATP酶活性以及血小板聚集过程的影响。通过ELISA技术发现两种肌球蛋白与其各自抗体之间存在强烈的交叉反应性。发现抗体优先结合肌球蛋白的“头部”片段，因为纯化的肌球蛋白“杆”与这两种抗体的反应较弱。两种抗肌球蛋白抗体强烈抑制两种肌球蛋白的K+(EDTA)ATP酶活性以及分离的肌球蛋白“头部”的活性。抑制上述酶活性所需的抗膜肌球蛋白抗体量比抗细胞质肌球蛋白抗体量小。两种抗体的F(ab)2片段也观察到类似结果。尽管这些抗体或其F(ab)2片段对血小板肌球蛋白ATP酶活性有强烈抑制作用，但未观察到它们对各种激动剂诱导的血小板聚集有影响。
