Cloning, expression and purification of Helicobater pylori L-asparaginase

   
Gladilina Yu.A.1 , Sokolov N.N.1, Krasotkina J.1

1. Orekhovich Institute of Biomedical Сhemistry RAMS
Section: Short Communication
PubMed Id: 18988465
Year: 2008  Volume: 54  Issue: 4  Pages: 482-486
Asparaginase from Helicobacter pylori has been cloned and expressed in E. coli cells. Optimization of culturing and expression conditions allowed achieving stable synthesis of catalytically active asparaginase amounting up to 6% of total bacterial protein. A method developed for enzyme purification included a single chromatographic stage and provided more than sixty percent yield of homogeneous asparaginase. Specific asparaginase and glutaminase activities were estimated to 92 and 8,310-3 ME/mg respectively. Due to low glutaminase specificity HpA may be employed as a non-toxic drug for leukemia treatment.
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Gladilina Yu.A., Sokolov N.N., Krasotkina J. (2008) Biomeditsinskaya khimiya, 54(4), 482-486.
This paper is also available as the English translation:10.1134/S1990750809010132
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