Isolation of Cx-Reactive Protein by Gel Filtration and Characterization by Electrophoresis and Immunodiffusion

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Abstract
Summary: A simple and mild procedure circumventing the use of pneumococcal Cx-polysaccharide for the isolation and purification of CxRP from rabbit acute phase serum has been described. This has been achieved by two passages through Sephadex G 200 of the crude CxRP obtained by precipitation with (NH4)2SO4. The purified CxRP characterized by electrophoresis and immunodiffusion appears to be a carbohydrate containing protein. Its relationship to CRP was shown by immunodiffusion with goat and horse CxRPA. It can be concluded that CxRP as it occurs in acute phase serum might be a complex entity.