Isolation and characterization of C-reactive protein from the dog

Immunology. 1984 Oct;53(2):307-13.


Using calcium-dependent affinity chromatography on Sepharose-bearing, covalently-coupled pneumococcal C-polysaccharide, a protein was isolated from the serum of dogs that had undergone general anaesthesia and major surgery. This protein was confirmed as the canine analogue of C-reactive protein (CRP) in other species by virtue of its electron microscopic appearance, subunit composition and behaviour as an acute phase reactant. Dog CRP had an apparent molecular weight of approximately 100,000 and was composed of five subunits of approximately 20,000 MW each. Two of the five subunits in each molecule were glycosylated. Negatively stained preparations had the typical cyclic pentameric disc-like structure of proteins of the pentraxin family, and in some preparations had a tendency to form stacks. Serum from normal healthy dogs of various strains usually contained less than 5 mg/l of CRP but, following the stimulus of major surgery, an increase in the CRP concentration was first detected at 4 hr.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • C-Reactive Protein / analysis
  • C-Reactive Protein / immunology
  • C-Reactive Protein / isolation & purification*
  • Chromatography, Gel
  • Dogs / blood*
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Glycoproteins / analysis
  • Immune Sera / immunology
  • Isoelectric Focusing
  • Male
  • Microscopy, Electron
  • Molecular Weight


  • Glycoproteins
  • Immune Sera
  • C-Reactive Protein