MUELLER-EBERHARD H J, LEPOW I H
J Exp Med. 1965 May 1;121(5):819-33. doi: 10.1084/jem.121.5.819.
Highly purified C'1 esterase of human serum is capable of inactivating isolated fourth component of human complement (beta(1E)-globulin). Inactivation is accompanied by changes in electrophoretic and ultracentrifugal properties of beta(1E)-globulin. If non-sensitized sheep erythrocytes are present during the action of C'1 esterase on beta(1E)-globulin, a complex is formed consisting of cells and cytolytically active fourth component (EC'4). Thus, inactivation of beta(1E)-globulin by C'1 esterase appears to be preceded by a state of activation enabling beta(1E)-molecules to combine with cell membrane receptors. Acceptor groups appear to be present also in 7S gamma-globulin and in beta(1E)-globulin itself, since C'1 esterase can induce the formation of beta-beta and of beta(1E)-7S gamma-globulin complexes.
高度纯化的人血清C'1酯酶能够使分离出的人补体第四成分(β(1E)-球蛋白)失活。失活过程伴随着β(1E)-球蛋白电泳和超速离心性质的变化。如果在C'1酯酶作用于β(1E)-球蛋白的过程中存在未致敏的绵羊红细胞,就会形成一种由细胞和具有溶细胞活性的第四成分(EC'4)组成的复合物。因此,C'1酯酶使β(1E)-球蛋白失活之前似乎先有一个激活状态,使β(1E)-分子能够与细胞膜受体结合。7Sγ-球蛋白和β(1E)-球蛋白本身似乎也存在受体基团,因为C'1酯酶能够诱导β-β和β(1E)-7Sγ-球蛋白复合物的形成。