Proteolysis of bovine immunoglobulins.
Bovine serum IgG1, colostral IgG1 and serum IgG2 with anti-ferritin activity were digested with pepsin or trypsin. Their fragments were characterized by immunoelectrophoresis, gel electrophoresis and gel filtration; their ferritin-binding ability was determined. The kinetics of proteolysis were established by measuring the appearance of free amino groups. No differences were observed between serum and colostrum IgG1. IgG1 was more susceptible to pepsin, and IgG2 to trypsin. This became evident from both the amount of intact IgG determined by gel electrophoresis, immunoelectrophoresis or gel filtration, and from the kinetics of the appearance of amino groups. A model is presented to explain the size, mobilities and properties of the obtained fragments.
D000818:Animals; D001345:Autoradiography; D002417:Cattle; D002850:Chromatography, Gel; D003126:Colostrum / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007122:Immunoelectrophoresis; D007074:Immunoglobulin G / Q000032:analysis; D008970:Molecular Weight; D010434:Pepsin A / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology*; D014357:Trypsin / Q000494:pharmacology
D007074:Immunoglobulin G; D010447:Peptide Hydrolases; D014357:Trypsin; D010434:Pepsin A