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.
Download PDF:  
Citation:

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). Purification and some properties of recombinant Erwinia carotovora L-asparaginase, expressed in E.coli cells. Biomeditsinskaya Khimiya, 49(5), 502-507.
References  
 2024 (vol 70)
 2023 (vol 69)
 2022 (vol 68)
 2021 (vol 67)
 2020 (vol 66)
 2019 (vol 65)
 2018 (vol 64)
 2017 (vol 63)
 2016 (vol 62)
 2015 (vol 61)
 2014 (vol 60)
 2013 (vol 59)
 2012 (vol 58)
 2011 (vol 57)
 2010 (vol 56)
 2009 (vol 55)
 2008 (vol 54)
 2007 (vol 53)
 2006 (vol 52)
 2005 (vol 51)
 2004 (vol 50)
 2003 (vol 49)