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

   
Borisova A.A.1, Eldarov M.A.2, Zgoon A.A.2, Alexandrova S.S.1, Omelyanuk N.M.1, Sokov B.N.3, Berezov T.T.4, Sokolov N.N.1

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
Section: Short Communication
PubMed Id: 16119104
Year: 2003  Volume: 49  Issue: 5  Pages: 502-507
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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Borisova A.A., Eldarov M.A., Zgoon A.A., Alexandrova S.S., Omelyanuk N.M., Sokov B.N., Berezov T.T., Sokolov N.N. (2003) Biomeditsinskaya khimiya, 49(5), 502-507.
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