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|Title:||Expression studies on antimicrobial protein, human beta defensin 25 fused with GST||Authors:||Er, Clarice Ru Hui||Keywords:||DRNTU::Engineering::Chemical engineering::Biotechnology||Issue Date:||2009||Abstract:||Human β-Defensin 25 (HBD-25) is a novel cationic antimicrobial peptide found in high abundance in male genital tract. The broad spectra of the antimicrobial activity of HBD against microbes make it a potential therapeutic agent in treatment against increasing antibiotic resistance in humans towards bacteria infection. Therefore, the expression of high yield and purity of HBD-25 using Ecoli as host cells will be desirable in order to facilitate clinical studies on HBD-25. The harmful effects of the expression of HBD-25 on the Ecoli had been avoided by attaching a fusion tag to the N-terminal of HBD-25. Glutathione S-Transferase (GST) is selected as the fusion tag to enhance the solubility of fusion protein.In this project, the expression conditions required for high yield and purity of GST-HBD-25 were investigated.||URI:||http://hdl.handle.net/10356/16392||Rights:||Nanyang Technological University||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SCBE Student Reports (FYP/IA/PA/PI)|
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