The Journal of Immunology · 1966 · 103 citations · 0 references
Life SciencesAnimal SciencesImmunologyComparative ImmunologyNutritional ImmunologyRuminant MedicineAntibody CharacterizationAntibody PurificationColostrum CompositionImmunoglobulin DiversityImmunoglobulin FunctionVeterinary ImmunologyElectrophoretic MobilityImmunoglobulin Class ProfilesImmunoglobulin TypingImmunoglobulins In ColostrumSedimentation Coefficient Analysis
Summary An immunoglobulin was isolated from rabbit colostrum which differed from γG-immunoglobulin in its β-electrophoretic mobility, content of unique antigenic sites, higher sedimentation coefficient (10.8S) and higher carbohydrate content (3.2% hexose and 3.2% hexosamine). The colostral immunoglobulin appeared to be homologous with γA-immunoglobulins of other species. A yield of 3 to 4.5 mg of γA-immunoglobulin was obtained per milliliter of colostrum. The rabbit γA-immunoglobulin was used to prepare a specific anti-α chain reagent in the goat. The serum concentration of γA-immunoglobulin was found to be 55 to 217 µg/ml for various rabbits by quantitative precipitation with anti-α chain. The Ab4 allotypic sites controlled by the b locus were present on γA-immunoglobulin but allotypic sites controlled by the a locus (Aa1 and Aa2) could not be identified on this protein.