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  • Title: [Purification of deamidase AG (asparaginase-glutaminase) from Pseudomonas fluorescens AG and some physicochemical properties of the enzyme].
    Author: Mardashev SR, Nikolaev AIa, Kovalenko NA, Rakov SS, Tsvetkova TA.
    Journal: Vopr Med Khim; 1975; 21(1):29-35. PubMed ID: 804211.
    Abstract:
    Deamidase AG (asparaginase-glutaminase) was obtained from Pseudomonas fluorescens in a crystalline apparently homogenous state. Molecular weight of the enzyme, determined by acrylamide gel electrophoresis, was equal to 128 000 daltons; by ultracentrifugation (56100 rev/min, 65 min, 20.5 degrees C) coefficient of sedimentation was shown to be 7.36 S. Optimal pH for asparaginase activity of the enzyme was at pH 8.0-9.0, for glutaminase activity--at pH 5.5-7.5.
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