[Cloning, expression and purification of Helicobater pylori L-asparaginase].
Asparaginase from Helicobacterpylori 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 x 10(-3) ME/mg respectively. Due to low glutaminase specificity HpA may be employed as a non-toxic drug for leukemia treatment.
Gladilina
Iu A
IuA
Sokolov
N N
NN
Krasotkina
Iu V
IuV
D000970:Antineoplastic Agents / Q000627:therapeutic use; D001215:Asparaginase / Q000096:biosynthesis* / Q000235:genetics; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics; D003001:Cloning, Molecular; D016480:Helicobacter pylori / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D007938:Leukemia / Q000188:drug therapy; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics
D000970:Antineoplastic Agents; D001426:Bacterial Proteins; D011994:Recombinant Proteins; D001215:Asparaginase