BINDING OF CANINE IGM AND IGG TO PROTEIN-A OF STAPHYLOCOCCUS-AUREUS - SIMPLE METHOD FOR THE ISOLATION OF CANINE IMMUNOGLOBULINS FROM SERUM AND THE LYMPHOCYTE SURFACE

  • 1 January 1979
    • journal article
    • research article
    • Vol. 40  (7) , 922-926
Abstract
The binding of normal canine serum Ig[immunoglobulin]G and IgM to staphylococcal protein A is described. Virtually all (> 99%) of IgG and up to 90% of IgM could be removed from canine serum, utilizing this phenomenon. The nature of the bound material was confirmed by immunodiffusion in agar, radioimmunoassay and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Attempts to elute differentially IgG and IgM from protein A-Sepharose columns, using gradients of pH or the chaotropic agent sodium thiocyanate, were unsuccessful. This phenomenon provides a basis for the isolation of canine IgM from serum. Lymphocyte surface IgM, studied by lactoperoxidase-catalyzed membrane radioiodination and solubilization in nonionic detergent, also showed the property of binding to staphylococcal protein A.