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| http://purl.uniprot.org/citations/14280442 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
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| http://purl.uniprot.org/citations/14280442 | http://purl.uniprot.org/core/author | "LEPOW I.H."xsd:string |
| http://purl.uniprot.org/citations/14280442 | http://purl.uniprot.org/core/author | "MUELLER-EBERHARD H.J."xsd:string |
| http://purl.uniprot.org/citations/14280442 | http://purl.uniprot.org/core/date | "1965"xsd:gYear |
| http://purl.uniprot.org/citations/14280442 | http://purl.uniprot.org/core/name | "J Exp Med"xsd:string |
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| http://purl.uniprot.org/citations/14280442 | http://purl.uniprot.org/core/title | "C'1 ESTERASE EFFECT ON ACTIVITY AND PHYSICOCHEMICAL PROPERTIES OF THE FOURTH COMPONENT OF COMPLEMENT."xsd:string |
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