C-reactive protein and serum amyloid P component in the plaice (Pleuronectes platessa L.), a marine teleost, are homologous with their human counterparts.
C-reactive protein and serum amyloid P component were isolated from serum of the plaice (Pleuronectes platessa L.), a murine teleost. The isolation was based on their calcium-dependent binding affinity for pneumococcal C-polysaccharide and for agarose, respectively. These specificities are the same as those of human C-reactive protein and serum amyloid P component, respectively, and we have previously reported that the plaice molecules resemble human C-reactive protein and serum amyloid P component in their electron microscopic appearance. We describe here estimation of the molecular weights of plaice C-reactive protein and serum amyloid P component and their subunits, and analysis of their amino acid composition, glycosylation and partial amino-terminal amino acid sequences. The results establish that plaice C-reactive protein and serum amyloid P component are homologous with each other and with their human counterparts and indicate that there has been stable conservation of this protein family throughout vertebrate evolution.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D002097:C-Reactive Protein / Q000276:immunology / Q000302:isolation & purification*; D002241:Carbohydrates / Q000032:analysis; D005399:Fishes / Q000097:blood*; D006801:Humans; D008970:Molecular Weight; D000683:Serum Amyloid P-Component
D000596:Amino Acids; D000682:Amyloid; D002241:Carbohydrates; D000683:Serum Amyloid P-Component; D002097:C-Reactive Protein