Heating at 56oC does not Eliminate Immune Complex-bound Clq

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Abstract
The effect of heating at 56.degree. C on free and complex-bound human C1q [q fragment of complement component] was studied by radioisotope and sucrose gradient centrifugation techniques. The ability of soluble complexes of egg albumin, rabbit anti-egg albumin and human C1q to bind extrinsic iodinated C1q did not increase following heating at 56.degree. C. The postulated release of complex-bound C1q on heating at 56.degree. C was not supported. Free C1q was more heat-labile than C1q in the C1qrs state. The importance of elimination or monitoring of intrinsic C1q in C1q assays for circulating immune complexes is stressed.