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  • Title: [Aminopeptidase system of Aspergillus flavus].
    Author: Tsyperovich AS, Kolodzeĭskaia MV, Konoplich LA.
    Journal: Ukr Biokhim Zh; 1977; 49(1):101-6. PubMed ID: 405779.
    Abstract:
    The aminopeptidases system contained in a complex of exocellular peptidhydrolases synthetized by Asp. flavus was studied. Separation of the system into individual enzymes of the type of leucin aminopeptidase, aminotripeptidase and specific leucyl-glycyl-glycine-aminopeptidase by the methods of salt fractionation. DEAE-Sephadex A-50 and DEAE-cellulose chromatography. These enzymes are characterized by a different degree of purification as well as by the presence of the multiple forms, anion and cation ones. The multiple forms differ in solubility, specific activity, chromatographic properties, thermostability. The presence of individual triglycine-aminotripeptidase is shown in the system. The differences are found in the properties of the enzymes splitting leucinamide and leucyl-glycine. There may be two different leucine aminopeptidases. Studies in correlation during hydrolysis of leucinamide and leucyl-glycyl-glycine and comparison of the fractions properties displaying the activities showed that there are no reasons to ascribe these both reactions to the effect of the same enzyme.
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