Abstract
Different forms of C-reactive proteins have been purified to electrophoretic homogeneity by calcium dependent affinity chromatography on a phosphorylcholine (PC)–Sepharose column from the sera of Labeo rohita confined in fresh water (CRPN) and water polluted with sublethal doses of cadmium (CRPCd), mercury (CRPHg), phenol (CRPPh), and hexachlorocyclohexane (CRPHx), which elevate serum CRP levels by three- to fivefold. On native PAGE, induced forms of CRP show remarkable differences in their electrophoteric mobility indicating differences in molecular mass, charge, and/or shape. Kinetic studies reveal the appearance of a pollutant specific molecular variant, which replaces the normal form at the peak of induction. Studies on amino acid and carbohydrate compositions, isoelectric focusing, binding to PC, C-polysaccharide (CPS) & lectins, and secondary structures of the purified CRPs, indicate, that, they differ significantly from each other, but grossly share the common properties of a CRP, including pentraxin, structure revealed by electron microscopy.
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