C-reactive protein and serum amyloid P component in the plaice (Pleuronectes platessa L.), a marine teleost, are homologous with their human counterparts

Mark B. Pepys, Frederick C. De Beer, Celia P. Milstein, John F. March, Arnold Feinstein, Neville Butress, John R. Clamp, Jackie Taylor, Christopher Bruton, Thelma C. Fletcher

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

C-reactive protein and serum amyloid P component were isolated from serum of the plaice (Pleuronectes platessa L.), a marine 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.

Original languageEnglish
Pages (from-to)123-133
Number of pages11
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume704
Issue number1
DOIs
StatePublished - May 21 1982

Bibliographical note

Funding Information:
This work was supported by MRC Programme Grant G979/51 to MBP. We thank Miss Joan Robins for expert secretarial assistance.

Keywords

  • (Teleost, Human)
  • Amyloid P
  • C-reactive protein
  • Evolution
  • Protein homology

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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