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Expression and purification of recombinant histidine-tagged L-asparaginase II from escherichia coli / Mohamed Gamal Salah Farahat ; Supervised Zienat Kamel Mohamed Ibrahim , AlaaEddeen Seufi Mohamed , Sherif Mohamed Elnagdy

By: Contributor(s): Material type: TextTextLanguage: English Publication details: Cairo : Mohamed Gamal Salah Farahat , 2014Description: 178 P. : charts , facsimiles ; 25cmOther title:
  • معاد الاتحاد المعلم بالهيستيدين من الايشيريشيا كولاى IIتعبير وتنقية ل-اسبراجيناز [Added title page title]
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Dissertation note: Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Botany Microbiology Summary: L-asparaginase (L-ASNase) has been widely used as a therapeutic agent in the treatment of various lymphoblastic leukemia diseases. In this study, Escherichia coli MG27 was isolated from the River Nile and subjected to optimization studies to maximize the production of L-ASNase. ansB gene, encoding L-ASNase II from E. coli MG27, was cloned into pQE-30 expression vector and expressed in E. coli M15. The recombinant histidine-tagged L-ASNase II was purified to homogeneity by Ni{u2013}NTA affinity chromatography and displayed a single 36.0 kDa band on SDS-PAGE
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Item type Current library Home library Call number Copy number Status Date due Barcode
Thesis Thesis قاعة الرسائل الجامعية - الدور الاول المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.05.Ph.D.2014.Mo.E (Browse shelf(Opens below)) Not for loan 01010110064452000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.05.Ph.D.2014.Mo.E (Browse shelf(Opens below)) 64452.CD Not for loan 01020110064452000

Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Botany Microbiology

L-asparaginase (L-ASNase) has been widely used as a therapeutic agent in the treatment of various lymphoblastic leukemia diseases. In this study, Escherichia coli MG27 was isolated from the River Nile and subjected to optimization studies to maximize the production of L-ASNase. ansB gene, encoding L-ASNase II from E. coli MG27, was cloned into pQE-30 expression vector and expressed in E. coli M15. The recombinant histidine-tagged L-ASNase II was purified to homogeneity by Ni{u2013}NTA affinity chromatography and displayed a single 36.0 kDa band on SDS-PAGE

Issued also as CD

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