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Issue:
Volume 54, issue 4

Title: CLONING, EXPRESSION AND PURIFICATION OF HELICOBATER PYLORI L-ASPARAGINASE

Authors: Yu.A. Gladilina, N.N. Sokolov, J. Krasotkina

Address:

Orekhovich Institute of Biomedical Сhemistry RAMS, Moscow; tel./fax: (495) 246-3380; e-mail: biomed_2005@bk.ru.

 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 8,3•10^-3 ME/mg respectively. Due to low glutaminase specificity HpA may be employed as a non-toxic drug for leukemia treatment.

Key words: recombinant L-asparaginase, acute lymphoblastic leucosis, Helicobacter pylori.

Биомедицинская химия, 2008 том 54, вып. 4, с. 482-486.

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