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  • Title: [Purification and properties of recombinant Erwinia carotovora L-asparaginase expressed in E.coli cells].
    Author: Borisova AA, El'darov MA, Zhgun AA, Aleksandrova SS, Omel'ianiuk NM, Sokov BN, Berezov TT, Sokolov NN.
    Journal: Biomed Khim; 2003; 49(5):502-7. PubMed ID: 16119104.
    Abstract:
    The method of purification Erwinia carotovora recombinant L-asparaginase, expressed in E.coli, including ultrasonic disintegration of biomass, fractionation ammonium sulfate and column chromatography on CM- or SP-Sepharose has been developed. According to SDS-PAAGE the enzyme preparation was homogeneous, its specific activity and yield consist respectively about 620 IU/mg of protein and 75%. Physical-chemical and structural properties of recombinant Erwinia carotovora L-asparaginase are similar to the enzymes from the wild strains Erwinia carotovora and recombinant L-asparaginase Erwinia chrysanthemi.
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