Amino acid sequence homology between rat and human C-reactive protein

J. A. Taylor, C. J. Bruton, J. K. Anderson, J. E. Mole, F. C. De Beer, M. L. Baltz, M. B. Pepys

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The rat serum protein that undergoes Ca2+-dependent binding to pneumococcal C-polysaccharide and to phosphocholine residues, and that is evidently a member of the pentraxin family of proteins by virtue of its appearance under the electron microscope, has been variously designated as rat C-reactive protein (CRP) and rat serum amyloid P component (SAP). The partial amino acid sequence (45 residues) towards the C-terminus of this protein was determined, and it showed 71.7% identity with the known sequence of human CRP but only 54.3% identity with human SAP. Since human CRP and SAP are themselves approximately 50% homologous, the level of identity between the rat protein and human SAP is evidence only of membership of the pentraxin family. In contrast, the much greater resemblance to human CRP confirms that the rat C-polysaccharide-binding/phosphocholine-binding protein is in fact rat CRP.

Original languageEnglish
Pages (from-to)903-906
Number of pages4
JournalBiochemical Journal
Volume221
Issue number3
DOIs
StatePublished - 1984

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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