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.
Gladilina Yu.A., Sokolov N.N., Krasotkina J. (2008) Cloning, expression and purification of Helicobater pylori L-asparaginase. Biomeditsinskaya Khimiya, 54(4), 482-486.
Gladilina Yu.A. et al. Cloning, expression and purification of Helicobater pylori L-asparaginase // Biomeditsinskaya Khimiya. - 2008. - V. 54. -N 4. - P. 482-486.
Gladilina Yu.A. et al., "Cloning, expression and purification of Helicobater pylori L-asparaginase." Biomeditsinskaya Khimiya 54.4 (2008): 482-486.
Gladilina, Yu. A., Sokolov, N. N., Krasotkina, J. (2008). Cloning, expression and purification of Helicobater pylori L-asparaginase. Biomeditsinskaya Khimiya, 54(4), 482-486.
