Purification of human C-reactive protein by immunoaffinity chromatography using mouse monoclonal antibody.

ABSTRACT

Human C-reactive protein (CRP) was purified from sera with a high concentration of CRP by immunoaffinity chromatography using mouse monoclonal antibody (mAb) to CRP (No. 18) and ion exchange on DEAE-Sephacel. CRP bound to the immunoaffinity column was eluted by 0.5 M acetate buffer, pH 5.0 containing 1.5 M NaCl. Final recovery of CRP was 90%. No significant immunochemical differences were observed between CRP obtained by the immunoaffinity chromatography and CRP purified by the method of Hokama and Riley.