Immunochemical studies on the combining sites of bovine immunoglobulins reactive with invertase.
Calcium-dependent and -independent bovine IgG reactive with invertase were isolated by affinity chromatography on invertase-coupled Sepharose 4B and their specificities were determined by competitive binding assays. The binding of 125I-labeled calcium-dependent and -independent bovine IgG reactive with invertase to invertase-coupled Sepharose 4B were most effectively inhibited by invertase and mannan. The binding was more weakly inhibited by mannose, glucose, and methyl alpha-D-mannopyranoside, whereas that was much more weakly inhibited by other monosaccharides and glycoproteins. These findings suggest that the combining sites of calcium-dependent and -independent bovine IgG reactive with invertase may be specific for invertase and/or mannan.
Sugii
S
S
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Japan.
Hirota
Y
Y
D000818:Animals; D000918:Antibody Specificity; D001667:Binding, Competitive; D002417:Cattle; D002846:Chromatography, Affinity; D006026:Glycoside Hydrolases / Q000378:metabolism*; D007074:Immunoglobulin G / Q000302:isolation & purification / Q000378:metabolism; D007136:Immunoglobulins / Q000302:isolation & purification / Q000378:metabolism*; D043324:beta-Fructofuranosidase
D007074:Immunoglobulin G; D007136:Immunoglobulins; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase