title: [Physicochemical and enzymatic properties of Aspergillus oryzae aminopeptidase].
abstract: The paper deals with properties of Aspergillus oryzae (strain KC) purified aminopeptidase. The enzyme is homogeneous in electrophoresis in polyacrylamide gel and enzyme-electrophoresis with the synthetic substrate leucyl-beta-naphthylamide applied. The molecular mass is 60000-61000 Daltons. The amino acidic composition of the enzyme is characterized by a high content of dicarboxylic acids. The substrate specificity is studied. Leucyl-glycyl-glycin and leucinamide are most intensive in splitting. Peptides with a blocked amino group are not hydrolyzed.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000378:metabolism*; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D000626:Aminopeptidases
vernacular_title: Fiziko-khimicheskie i enzimaticheskie svoistva aminopeptidazy Aspergillus oryzae.