Purification and characterization of canine collagens I and II

The purpose of this study was to demonstrate that commercially available hu man anti-collagen antibodies are suitable for use with canine tissues. This paper describes a reproducible procedure for isolating and purifying canin e skin and cartilage collagens in quantities sufficient to characterize. Th e skin and cartilage were readily dissolved in dilute acetic acid with peps in, and the collagens were purified by salt precipitation. Purified collage ns were characterized by sodium dodecyl sulfate-polyacrylamide gel electrop horesis (SDS-PAGE) and by immunodetection on electroblot. The tissue distri bution of the canine collagens was examined by immunohistochemistry. Two po lypeptide chains were identified by SDS-PAGE in the canine skin sample and a human collage Type I control. One polypeptide chain was identified in the canine articular cartilage sample and a human collagen Type II control. Im munoblotting revealed the individual components for the collagen antigens. Anti-human Type II collagen immunoreacted specifically with cells of a chon drocytic phenotype. Antihuman Type I collagen appeared to be less specific. Because the antibodies exhibited cross-species reactivity, homology betwee n canine Type I and II: collagens and human Type I and II collagens is sugg ested. Commercial antibodies for human collagens Type I and II are suitable for study of these canine collagens.