Purification and some properties of recombinant erwinia carotovora L-asparaginase, expressed in E.coli cells

   


1. Institute of Biomedical Chemistry RAMS
2. Center of Bioengineering, Russian Academy of Sciences
3. RCT&HRB The Ministry of Health of the Russian Federation
4. Peoples' Frendship University
Type: Short communication
PubMed Id: 16119104
Year: 2003 vol: 49  issue:5  pages: 502-507
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 СМ- 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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Reference: Borisova A.A., Eldarov M.A., Zgoon A.A., Alexandrova S.S., Omelyanuk N.M., Sokov B.N., Berezov T.T., Sokolov N.N., Purification and some properties of recombinant erwinia carotovora L-asparaginase, expressed in E.coli cells, Biomeditsinskaya khimiya, 2003, vol: 49(5), 502-507.
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