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

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.

Authors
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
Journal
Biomeditsinskaya Khimiya
Publisher
Russian Academy of Medical Sciences
Number of issue
5
Language
Russian
Pages
502-507
Status
Published
Link
External link
Volume
49
Year
2003
Organizations
  • 1 Inst. of Biomedical Chemistry RAMS, Pogodinskaya str., Moscow, 119121, Russian Federation
  • 2 Center of Bioengineering, Russian Academy of Sciences, Prospio 60-letya Oktyabrya, 7/1, Moscow, 117312, Russian Federation
  • 3 RCT and HRB, Min. of Hlth. of the Rus. Federation, Lenin str., 102A, Serpukhov, Moscow Region, 142253, Russian Federation
  • 4 Peoples' Frendship University, Miklucho-Maklaya str. 6, Moscow, 117178, Russian Federation
Keywords
E.coli; Erwinia carotovora; L-asparaginase; Leukemia; Recombinant proteins
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