Perret B A, Furlan M, Beck E A
Agents Actions. 1981 Dec;11(6-7):657-9. doi: 10.1007/BF01978784.
Bovine factor VIII/platelet aggregating factor was adsorbed into gold granules and the protein-gold complex added to either formalin-fixed or fresh washed human platelets. Following aggregation, binding of gold granules to the platelets was measured by monitoring the optical density of colloidal gold remaining in the supernatant. Scatchard analysis of binding data indicated that multiple classes of binding sites were present. The number of high affinity binding sites per formalin-fixed platelet depended on the concentration of ristocetin: 420 gold granules were calculated to bind at 1.4 mg/ml of ristocetin, 610 at 0.6 mg/ml of ristocetin and 875 when no ristocetin was added. Fresh washed platelets bound 1350 granules per cell in the absence of ristocetin. We conclude that during platelet aggregation, induced by bovine factor VIII, the binding sites on the platelet surface are only partially occupied.
牛因子VIII/血小板聚集因子被吸附到金颗粒上，然后将蛋白质-金复合物添加到福尔马林固定或新鲜洗涤的人血小板中。聚集后，通过监测上清液中剩余胶体金的光密度来测量金颗粒与血小板的结合。对结合数据的Scatchard分析表明存在多类结合位点。每个福尔马林固定血小板上高亲和力结合位点的数量取决于瑞斯托霉素的浓度：计算得出，在1.4mg/ml瑞斯托霉素时，有420个金颗粒结合；在0.6mg/ml瑞斯托霉素时，有610个；不添加瑞斯托霉素时，有875个。在没有瑞斯托霉素的情况下，新鲜洗涤的血小板每个细胞结合1350个颗粒。我们得出结论，在牛因子VIII诱导的血小板聚集过程中，血小板表面的结合位点仅被部分占据。
