Abstract
Highly purified C'1 esterase of human serum is capable of inactivating isolated fourth component of human complement (β1E-globulin). Inactivation is accompanied by changes in electrophoretic and ultracentrifugal properties of β1E-globulin. If non-sensitized sheep erythrocytes are present during the action of C'1 esterase on β1E-globulin, a complex is formed consisting of cells and cytolytically active fourth component (EC'4). Thus, inactivation of β1E-globulin by C'1 esterase appears to be preceded by a state of activation enabling β1E-molecules to combine with cell membrane receptors. Acceptor groups appear to be present also in 7S γ-globulin and in β1E-globulin itself, since C'1 esterase can induce the formation of β-β and of β1E-7S γ-globulin complexes.
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