C1q has albumin binding activity but does not interfere in the hemagglutination test for anti-albumin antibodies.
Two factors in the sera of patients with liver disease interact with polymerized human serum albumin (HSAP). These are anti-albumin antibodies (AAA) and receptors for polymerized albumin on HBsAg. Recently it was demonstrated by radioimmunoassay that purified human C1q also binds HSAP. Our data confirm the reaction between purified human C1q and HSAP by passive hemagglutination and by indirect immunofluorescence of HSAP-coated erythrocytes (E-HSAP). It is shown that although purified C1q binds HSAP, in the serum, the AAA and not C1q are responsible for the albumin binding activity in HBsAg-negative sera of patients with liver disease and of normal individuals, as detected by passive hemagglutination of E-HSAP, AAA were found to inhibit the binding of serum C1q to polymerized albumin, and hence the E-HSAP hemagglutination test for AAA titration in human sera proved valid.
D000906:Antibodies / Q000032:analysis*; D001667:Binding, Competitive; D003166:Complement Activating Enzymes / Q000378:metabolism*; D015922:Complement C1q; D005455:Fluorescent Antibody Technique; D006386:Hemagglutination Tests; D006801:Humans; D008107:Liver Diseases / Q000097:blood; D012709:Serum Albumin / Q000276:immunology / Q000378:metabolism*
D000906:Antibodies; D012709:Serum Albumin; D015922:Complement C1q; D003166:Complement Activating Enzymes