Disulfide bridge formation between C1q and IgG in vitro.
The globular heads of C1q are known to possess free-SH groups. Here we show that these groups, which are concealed in the native molecule, are exposed by interaction of C1q with dialysis membrane. During iodination, I+ and I2 oxidize these sulfhydryls to produce disulfide-linked C1q aggregates. Approximately 15% of C1q bound to immunoglobulin aggregates is resistant to high conductivity elution and reducing agent is required to release it. These data show that dialysis, adsorption to Ig and iodination of C1q result in structural and functional changes in the molecule, and suggest a mechanism by which these changes occur. Disulfide bridging between C1q and IgG in vitro suggests that this may be a normal physiological function of C1q for which the free cysteines of human, mouse and guinea pig C1q have been conserved.
Martin
H
H
Kennedy Institute of Rheumatology, Hammersmith, London, GB.
Kaul
M
M
Loos
M
M
D000818:Animals; D003167:Complement Activation; D015922:Complement C1q; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006168:Guinea Pigs; D007074:Immunoglobulin G; D066298:In Vitro Techniques; D008297:Male; D013438:Sulfhydryl Compounds
D007074:Immunoglobulin G; D013438:Sulfhydryl Compounds; D015922:Complement C1q