Voprosy meditsinskoi khimii (ISSN 0042-8809)

Purification of deamidase AG (asparaginase-glutaminase) from Pseudomonas fluorescens AG and some physicochemical properties of the enzyme

   
Mardashev S.R., Nikolaev A.Ya., Kovalenko N.A., Rakov S.S., Tsvetkova T.A.
PubMed Id: 804211
Year: 1975 vol: 21  issue:1  pages: 29-35
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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Reference: Mardashev S.R., Nikolaev A.Ya., Kovalenko N.A., Rakov S.S., Tsvetkova T.A., Purification of deamidase AG (asparaginase-glutaminase) from Pseudomonas fluorescens AG and some physicochemical properties of the enzyme, Voprosy meditsinskoi khimii, 1975, vol: 21(1), 29-35.
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