RHP was purified from normal serum by sequential euglobin precipitation, ion exchange chromatography on DEAE-Sephacel and gel filtration using Sephacryl S-300. RHP reacted with anti-Factor H antibodies in ELISA assays and in Western blots, suggesting that it is antigenically related to Factor H. It bound to intact Clq but not to the collagen-like N-terminal half of the molecule. Clq-specific monoclonal antibody BUS-1, which blocks the binding of C1q to immune complexes, did not block the binding of RHP to C1q. This implies that the binding sites on C1q for IgG and RHP do not overlap. © 1992.