The plasma protein which inhibits complement-mediated prevention of immune precipitation is an Fc binding protein.
A glycoprotein (gp60) that inhibits complement-mediated prevention of immune precipitation (PIP) has been purified from normal serum. [125I]gp60 binds to IgG but not to IgA or IgM. The binding site has been shown to be localized on the Fc piece. The binding of radiolabelled gp60 to IgG has been analysed by direct binding and Scatchard, double-reciprocal and Hill plots. The mean affinity constant of gp60 for IgG is 1.56 x 10(8) l/mol and there appears to be a single class of binding sites for gp60 on IgG. Saturation was achieved when one molecule of gp60 was bound to each molecule of IgG. In competition inhibition assays, gp60 was shown to compete with C1q and IgM and IgG rheumatoid factors. The ability to inhibit C1q binding suggests that gp60 inhibits PIP by preventing binding and activation of C1. The possibility that gp60 is a fluid-phase Fc gamma receptor is discussed. See also the note added in proof.
Ahmed
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AE
University of Glasgow Department of Pathology, Western Infirmary, Glasgow, UK.
Bird
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P
McKay
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IC
Whaley
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K
D001665:Binding Sites; D001667:Binding, Competitive; D015922:Complement C1q / Q000378:metabolism*; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000378:metabolism*; D047468:Immunoprecipitation; D011485:Protein Binding; D012217:Rheumatoid Factor / Q000378:metabolism; D012795:Sialoglycoproteins / Q000378:metabolism*
D007141:Immunoglobulin Fc Fragments; D012795:Sialoglycoproteins; C065610:sialoglycoprotein gp60; D015922:Complement C1q; D012217:Rheumatoid Factor