The role of Fc:Fc interactions in insoluble immune complex formation and complement activation.
The initial rate of formation of insoluble immune complexes from rabbit IgG and ovalbumin was approximately 12 times that for formation of F(ab')2-ovalbumin complexes. At low IgG concns, in the range 0.7-2.7 nM, the formation of insoluble immune complexes was characterised by a lag phase, especially for complexes formed in low antigen excess, compared to antibody excess. Guanidine HCl (at concns up to 0.5 M) and urea (at concns up to 1 M) decreased the initial rates of formation of IgG immune complexes more than F(ab')2 immune complexes. Pre-formed IgG immune complexes were solubilised at lower guanidine HCl concns than were F(ab')2 immune complexes. C1q enhanced the initial rate of formation of IgG immune complexes at C1q:IgG ratios up to 1:1. Higher C1q concns decreased the initial rate of formation of the complexes. Urea (1 M) blocked the C1q mediated enhancement of immune complex formation.
Easterbrook-Smith
S B
SB
Department of Biochemistry, University of Sydney, Australia.
Vandenberg
R J
RJ
Alden
J R
JR
D000818:Animals; D000936:Antigen-Antibody Complex / Q000276:immunology*; D003167:Complement Activation; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D007141:Immunoglobulin Fc Fragments / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology; D010047:Ovalbumin / Q000276:immunology; D011489:Protein Denaturation; D012995:Solubility
D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D010047:Ovalbumin