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Structure - function relationship of two glutathione transferase isoenzymes purified from biomophalaria alexandrina snail / Ghada Soliman Ahmed ; Supervised Amr Saad Elsaid , Mohamed Ali Eldossoky , Abdelmonem Abdelhamid Ahmed

By: Contributor(s): Material type: TextTextLanguage: eng Publication details: Cairo : Ghada Soliman Ahmed , 2010Description: 147Leaves : charts , photographs ; 30cmOther title:
  • علاقة التركيب بالوظيفة لإثنين من ايزوانزيمات الجلوتاثيون ترانسفيريز المنقيين من قوقع البيوموفلاريا ألكساندرينا [Added title page title]
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Dissertation note: Thesis (M.Sc.) - Cairo University - Faculty of Science - Department of Biochemistry Summary: A simple reproducible procedure for the purification of the two major GST isoenzymes was established . The purification fold was 590.3 and 461.2 for GST2 and GST3, respectively . SDS - PAGE revealed that both isoenzymes are homodimers with subunit molecular weight equal 23.2 kDa. Kinetic studies of the two isoenzymes at different p{uFF28} values display a typical michaelis - behavior with respect to 1 - cloro -2, 4- dinitrobenzene and glutathione as substrate
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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 Cai01.12.02.M.Sc.2010.Gh.S (Browse shelf(Opens below)) Not for loan 01010110052645000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.02.M.Sc.2010.Gh.S (Browse shelf(Opens below)) 52645.CD Not for loan 01020110052645000

Thesis (M.Sc.) - Cairo University - Faculty of Science - Department of Biochemistry

A simple reproducible procedure for the purification of the two major GST isoenzymes was established . The purification fold was 590.3 and 461.2 for GST2 and GST3, respectively . SDS - PAGE revealed that both isoenzymes are homodimers with subunit molecular weight equal 23.2 kDa. Kinetic studies of the two isoenzymes at different p{uFF28} values display a typical michaelis - behavior with respect to 1 - cloro -2, 4- dinitrobenzene and glutathione as substrate

Issued also as CD

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