Rat Clq : Similarity to human Clq in functional and compositional properties

Abstract

Clq was purified from rat and human serum. Rat and human Clq were indistinguishable functionally as assessed by the capacity of isolated preparations to bind to aggregated IgG from either source. By polyacrylamide disc electrophoresis in the presence of sodium dodecyl sulphate, rat Clq exhibited two noncovalent subunits and, following reduction and alkylation, three smaller polypeptide chains, the apparent molecular weights of which were comparable to those of human Clq.