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From the Department of Molecular Immunology, Scripps Clinic and Research Foundation, 476 Prospect Street, La Jolla, California 92037
Abstract
Complement receptor activity for cell bound C3b and C3b was detected on plasma membrane fragments prepared by nitrogen cavitation from cultured human lymphoid cells. The activity of the membrane fragments reflected the activity of the whole cells in that cells which did not form rosettes (P3J and RPMI 4098) resulted in inactive membranes and cells with high rosette formation (NC37 and Raji) yielded highly active membrane fragments. Two test systems were devised to detect these receptor activities, namely a rosette inhibition and a hemagglutination assay. Solubilization of C3 receptors was accomplished by extraction of active plasma membrane fragments with 2 M KBr. dissociation and reassociation experiments suggest C3b and C3d receptors to be highly complex molecular structures. It appears that these complement receptors on plasma membranes rely on both protein and lipid moieties for the expression of their activity.
Footnotes
1 This is Publication No. 896 from the Department of Molecular Immunology, Scripps Clinic and Research Foundation. This work was supported by United States Public Health Service Grants AI 10180 and AI 07007 from the National Institutes of Health and Grant 70615 from the American Heart Association, Inc.
2 M. P. D. is a Visiting Scientist from the Institut für Medizinische Mikrobiologie, Johannes Gutenberg Universitat, Mainz, Germany. He is supported by the Deutsche Forschungsgemeinschaft, Bad Godesberg, Germany.
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