Heating at 56 degrees C does not eliminate immune complex-bound Clq.
The effect of heating at 56 degrees C on free and complex-bound Clq was studied by radioisotope and sucrose gradient centrifugation techniques. The ability of soluble complexes of egg albumin, rabbit anti-egg albumin, and human Clq to bind extrinsic iodinated Clq did not increase following heating at 56 degrees C. The results of this study did not support the postulated release of complex-bound Clq on heating at 56 degrees C. They also showed that free Clq was more heat-labile than Clq in the Clqrs state. The importance of elimination or monitoring of intrinsic Clq in Clq assays for circulating immune complexes is stressed.
D000818:Animals; D000936:Antigen-Antibody Complex; D002499:Centrifugation, Density Gradient; D003172:Complement C1 / Q000032:analysis / Q000276:immunology*; D006358:Hot Temperature; D006801:Humans; D011817:Rabbits; D011863:Radioimmunoassay
D000936:Antigen-Antibody Complex; D003172:Complement C1