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Isolation and characterization of antibacterial peptide from the mosquito, Aedes (ochlerotatus) caspius-diptera :Culicidae / Walaa Ibrahim Mahmoud Ahmed ; Supervsied Nehal Mohamed Elwan , Manal Bahaa Eldin Mahmoud

By: Contributor(s): Material type: TextTextLanguage: English Publication details: Cairo : Walaa Ibrahim Mahmoud Ahmed , 2016Description: 48 P. : cahrts ; 25cmOther title:
  • تنقية وتوصيف ببتيد مضاد للبكتيريا معزول من باعوضة آيديس (أوكليروتانوس) كاسبيس - ثٌائية الأجنحة :كيوليسيدى [Added title page title]
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  • Issued also as CD
Dissertation note: Thesis (M.Sc.) - Cairo University - Faculty of Science - Department of Biochemistry Summary: One antimicrobial peptide was isolated and purified to 5.5-fold purification from the crude lysate of immunized Aedes caspius larvae by (NH4) 2SO4 fractionation, ion-exchange chromatography, and reverse-phase high performance liquid chromatography (HPLC). The peptide, named ACAm, was found to be heat stable below 80{u00B0}C and attained the maximum antimicrobial activities at acidic pH range. The estimated molecular weight of ACAm by sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE), under non-reducing conditions, was 4 KDa. Using isoelectric focusing (IEF), ACAm exhibited pI in basic pH (8.4) belonging to cationic peptides. The hydrophobic amino acids represented 45.7% of the peptide where the calculated hydrophobicity indexwas 1.12. Both the crude extract and ACAm exhibited strong antimicrobial activities against gram- positive and Gram-negative bacteria as well as against peptidoglycans and lipopolysacchrides of bacterial cell walls
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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.2016.Wa.I (Browse shelf(Opens below)) Not for loan 01010110072103000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.12.02.M.Sc.2016.Wa.I (Browse shelf(Opens below)) 72103.CD Not for loan 01020110072103000

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

One antimicrobial peptide was isolated and purified to 5.5-fold purification from the crude lysate of immunized Aedes caspius larvae by (NH4) 2SO4 fractionation, ion-exchange chromatography, and reverse-phase high performance liquid chromatography (HPLC). The peptide, named ACAm, was found to be heat stable below 80{u00B0}C and attained the maximum antimicrobial activities at acidic pH range. The estimated molecular weight of ACAm by sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE), under non-reducing conditions, was 4 KDa. Using isoelectric focusing (IEF), ACAm exhibited pI in basic pH (8.4) belonging to cationic peptides. The hydrophobic amino acids represented 45.7% of the peptide where the calculated hydrophobicity indexwas 1.12. Both the crude extract and ACAm exhibited strong antimicrobial activities against gram- positive and Gram-negative bacteria as well as against peptidoglycans and lipopolysacchrides of bacterial cell walls

Issued also as CD

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