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  • Title: [Characteristics of extracellular proteolytic enzymes of Actinomyces fradiae 0072].
    Author: Kashkin AP, Voevodin IuN, Maklova TG.
    Journal: Prikl Biokhim Mikrobiol; 1976; 12(4):563-71. PubMed ID: 194235.
    Abstract:
    The composition of extracellular proteinases from Actinomyces fradiae 0072 and their effect on proteins and synthetic substrates were studied. The enzyme preparation was found to have keratinolytic, caseinolytic, collagenolytic, collagenase, trypsin-like, carboxy- and aminopeptidase activities. Five low molecular weight proteinases capable to hydrolyse keratin, casein, azocollagen were obtained via fractionation of the enzyme preparation on DEAE-cellulose and Sephadex columns. Proteinases from Act. fradiae and aminopeptidase with a molecular weight of 31,000 were shown to be different enzymes. In hydrolysis of L-leucyl-2-naphthylamide the Michaelis constant and Vmax of the enzyme were found to be 3.02 X 10(-3) M and 0.35 X 10(2) micronM/ml-min, respectively.
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