Immunochemical studies on α-amylase

摘要: Abstract Crystalline enzyme prepared from a crude concentrate of Aspergillus oryzae, and found to consist single antigenic component by various physicochemical immunochemical methods, was used produce rabbit antisera. The contribution some aspects the structure α-amylase antigen interaction with antienzyme examined. Exposure concentrated urea solutions under conditions resulted in preparations giving reactions partial identity native immunodiffusion analysis. Quantitative precipitin determinations employing urea-treated show that only loss reactivity occurs even prolonged treatment. After treatment EDTA presence 0.1 M mercaptoethanol also showed changes its reactivity. A comparison behavior specific activity before after leucine aminopeptidase or carboxypeptidase suggests neither N-terminal nor C-terminal amino acid residues play significant role enzymic