EFFECT OF LIMITED PROTEOLYSIS BY TRYPSIN AND CHYMOTRYPSIN ON BOVINE COLOSTRAL IGG1

  • 1 January 1977
    • journal article
    • research article
    • Vol. 32  (2) , 215-219
Abstract
Limited proteolysis of bovine colostral IgG1 [immunoglobulin G1] by trypsin caused loss of specific antibody activity but column chromatography showed that relatively little cleavage into fragments had occurred. Polyacrylamide-agarose SDS [sodium dodecyl sulfate] electrophoresis of the 2-mercaptoethanol-treated digest revealed that extensive cleavage of L chains had occurred, even though most of the material before reduction had a molecular weight close to that of undigested IgG1. Although a Fab-type fragment was detected in the digest by immunoelectrophoresis it appeared to be only a minor component. Chymotrypsin had little effect upon the structure or antibody activity of IgG1. These findings may explain the effect of trypsin and chymotrypsin on the bactericidal activity of colostral antibodies.