Primary structure of rabbit C-reactive protein.

Abstract

permitted the assignments of amino acid residues that might be involved in the binding of phosphorylcholine.In the presence of infectious diseases and various other pathological conditions there appears in the serum of man a protein not normally detected.This is called C-reactive protein because it has the curious property of precipitating with C-polysaccharide derived from the cell wall of Streptococcus pneumoniae (1).Proteins analogous to CRP' have been isolated from sera of other species (2-5) including an invertebrate, Limuluspolyphemus (6).Like immunoglobulins, CRP mediates in vitro many reactions, enhancing phagocytosis (7) and promoting precipitation of bacterial cells (1) and certain polymers (8).There is, however, no structural homology between CRP and immunoglobulins (9).The occurrence in the rabbit of an acute phase protein analogous to human CRP has been reported by Anderson and McCarty (2).Thus, an animal model exists for the study of the biochemical and physiological role of this protein.The present investigation was initiated to determine the primary