C'1 ESTERASE EFFECT ON ACTIVITY AND PHYSICOCHEMICAL PROPERTIES OF THE FOURTH COMPONENT OF COMPLEMENT

Abstract

Highly purified C'1 esterase of human serum is capable of inactivating isolated fourth component of human complement (ß1E-globulin). Inactivation is accompanied by changes in electrophoretic and ultracentrifugal properties of ß1E-globulin. If non-sensitized sheep erythrocytes are present during the action of C'1 esterase on ß1E-globulin, a complex is formed consisting of cells and cytolytically active fourth component (EC'4). Thus, inactivation of ß1E-globulin by C'1 esterase appears to be preceded by a state of activation enabling ß1E-molecules to combine with cell membrane receptors. Acceptor groups appear to be present also in 7S γ-globulin and in ß1E-globulin itself, since C'1 esterase can induce the formation of ß-ß and of ß1E-7S γ-globulin complexes.