Russian Journal
|
Russian Journal |
ISSN 0042-8809 |
| Biomeditsinskaya Khimiya | Biomedical Chemistry |
Issue:
Volume 49, issue 5
Title: PURIFICATION AND SOME PROPERTIES OF RECOMBINANT ERWINIA CAROTOVORA L-ASPARAGINASE, EXPRESSED IN E.COLI CELLS
Authors: A.A.Borisova1, M.A.Eldarov2, A.A.Zgoon2, S.S.Alexandrova1, N.M.Omelyanuk1, B.N.Sokov3, T.T.Berezov4, N.N.Sokolov1
Address:
1Institute of Biomedical Chemistry RAMS, Pogodinskaya str., Moscow, 119121Russia; phone/fax: (095)246-33-80/(095)245-08-57; e-mail: sokolov@ibmc.msk.ru
2Center of Bioengineering, Russian Academy of Sciences, Prospþ 60-letya Oktyabrya, 7/1, Moscow, 117312, Russia3RCT&HRB The Ministry of Health of the Russian Federation, Lenin str., 102A, Serpukhov, Moscow region, 142253, Russia
4Peoples' Frendship University, Miklucho-Maklaya str. 6, Moscow, 117178, Russia
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 ÑÌ- 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.
Key words: L-asparaginase, leukemia, recombinant proteins, Erwinia carotovora, E.coli.
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