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      Isolation of two C-reactive protein homologues from cod (Gadus morhua L.) serum.

      Fish & Shellfish Immunology
      Amino Acid Sequence, Animals, Antibodies, Monoclonal, metabolism, C-Reactive Protein, chemistry, isolation & purification, ultrastructure, Chromatography, Affinity, Chromatography, Ion Exchange, Fish Proteins, Gadus morhua, blood, immunology, Glycosylation, Ligands, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, Protein

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          Abstract

          Pentraxins are important molecules in innate defence and play a role in the acute phase response of both mammals and fish. Isolation of cod pentraxins by affinity chromatography using phosphorylcholine agarose revealed two pentraxin-like proteins, referred to as PI and PII proteins. These varied in their overall charge, pentameric and subunit molecular size, glycosylation and N-terminal amino acid sequences. The PI protein was homologous with the CRP-like pentraxin previously described in cod whereas the PII protein was a new CRP homologue, which was characterized by substantial individual heterogeneity with regard to subunit size and relative density. The results indicate considerable genetic variations in the cod pentraxins.

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