Cloning, expression and purification of Helicobater pylori L-asparaginase


1. Orekhovich Institute of Biomedical Сhemistry RAMS
Type: Short communication
PubMed Id: 18988465
Year: 2008 vol: 54  issue:4  pages: 482-486
Abstract: 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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Reference: Gladilina Yu.A., Sokolov N.N., Krasotkina J., Cloning, expression and purification of Helicobater pylori L-asparaginase, Biomeditsinskaya khimiya, 2008, vol: 54(4), 482-486.
This paper is also available as the English translation:10.1134/S1990750809010132