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.
Download PDF:
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.
Bibliography
 2016(Vol:62)
 2015(Vol:61)
 2014(Vol:60)
 2013(Vol:59)
 2012(Vol:58)
 2011(Vol:57)
 2010(Vol:56)
 2009(Vol:55)
 2008(Vol:54)
 2007(Vol:53)
 2006(Vol:52)
 2005(Vol:51)
 2004(Vol:50)
 2003(Vol:49)