Gogstad G O, Brosstad F
Thromb Res. 1983 Jan 15;29(2):237-41. doi: 10.1016/0049-3848(83)90145-7.
Crossed immunoelectrophoresis of platelets against antiplatelet antibodies has proved to be a valuable tool in the study of platelet proteins (1-8). The advantage of this separation system is that the proteins are separated under nondenaturating conditions and thus to some extent would be expected to maintain their functional properties. Previously, the binding of several proteins to immobilized thrombin (5) and immobilized heparin (9) during crossed immunoelectrophoresis of platelet proteins solubilized in a Triton X-loo-containing buffer has been described. Furthermore, it has been demonstrated that fibrinogen is able to bind to immunoprecipitates containing the glycoprotein IIb-IIIa-complex (7). These studies indicate that the proteins contained in the immunoprecipitates represent biologically active entities. In the present study we provide direct evidence for this by demonstrating enzymatic activity associated with the immunoprecipitate containing Factor XIII in immunoplates obtained after crossed immunoelectrophoresis of solubilized platelets against anti-platelet antibodies.
血小板与抗血小板抗体的交叉免疫电泳已被证明是研究血小板蛋白的一种有价值的工具(1 - 8)。这种分离系统的优点是蛋白质在非变性条件下分离，因此在某种程度上有望保持其功能特性。以前，已经描述了在含Triton X - 100缓冲液中溶解的血小板蛋白进行交叉免疫电泳时，几种蛋白质与固定化凝血酶(5)和固定化肝素(9)的结合。此外，已经证明纤维蛋白原能够与含有糖蛋白IIb - IIIa复合物的免疫沉淀物结合(7)。这些研究表明免疫沉淀物中所含的蛋白质代表生物活性实体。在本研究中，我们通过证明在溶解的血小板与抗血小板抗体进行交叉免疫电泳后获得的免疫板中，与含有因子XIII的免疫沉淀物相关的酶活性，为此提供了直接证据。
