ISOLATION AND CHARACTERIZATION OF C-REACTIVE PROTEIN FROM THE DOG

  • 1 January 1984
    • journal article
    • research article
    • Vol. 53  (2) , 307-313
Abstract
Using Ca-dependent affinity chromatography on Sepharose-bearing, covalently-coupled pneumococcal C-polysaccharide, a protein was isolated from the serum of dogs that had undergone general anesthesia and major surgery. This protein was confirmed as the canine analog of C-reactive protein (CRP) in other species by virtue of its EM appearance, subunit composition and behavior as an acute phase reactant. Dog CRP had an apparent MW of .apprx. 100,000 and was composed of 5 subunits of .apprx. 20,000 MW each. Two of the 5 subunits in each molecule were glycosylated. Negatively stained preparations had the typical cyclic pentameric disk-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 < 5 mg/l of CRP but, following the stimulus of major surgery, an increase in the CRP concentration was first detected at 4 h.