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Expression and purification of small peptides have always been problematic due to enzymatic degradation and many other technical problems. We report cloning and expression of a low molecular weight human antimicrobial peptide ?hepcidin' (Hepc, 20 amino acids) in pPIC9K transformed into P. pastoris GS115. The study reveals that active hepcidin peptide can be successfully expressed in this methylotrophic yeast. The BMMY medium was found to be optimal for the hepcidin protein expression and growth of the recombinant strains. Hepcidin protein expressed in recombinant strains was about 3 mg/L. Peptide expression was verified by Western blotting and ELISA assay. Recombinant hepc 20 was purified through Reverse-Phase HPLC column and characterized by Mass Spectrometry and amino acid sequencing. It also exhibited antibacterial activity against Staphylococcus aureus and Bacillus subtilis.
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Dr Farzana Rashid is Assistant Professor at the Lahore University. She has 14 research publications, nine international and four national on her credit in the field of biotechnology, microbiology and education.Dr. Farzana has experience in coordinating Teacher Education programs and her interest areas include education and research.
Dr Farzana Rashid is Assistant Professor at the Lahore University. She has 14 research publications, nine international and four national on her credit in the field of biotechnology, microbiology and education.Dr. Farzana has experience in coordinating Teacher Education programs and her interest areas include education and research.
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AN OPTIMIZED EXPRESSION OF RECOMBINANT HEPCIDIN
Editore:
VDM Verlag Dr. Müller, 2010
ISBN 10: 3639283244
ISBN 13: 9783639283242
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Da: moluna, Greven, Germania
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Kartoniert / Broschiert. Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Rashid FarzanaDr Farzana Rashid is Assistant Professor at the Lahore University. She has 14 research publications, nine international and four national on her credit in the field of biotechnology, microbiology and education.Dr. F. Codice articolo 4973912
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AN OPTIMIZED EXPRESSION OF RECOMBINANT HEPCIDIN : USING PICHIA PASTORIS
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Taschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Expression and purification of small peptides have always been problematic due to enzymatic degradation and many other technical problems. We report cloning and expression of a low molecular weight human antimicrobial peptide hepcidin' (Hepc, 20 amino acids) in pPIC9K transformed into P. pastoris GS115. The study reveals that active hepcidin peptide can be successfully expressed in this methylotrophic yeast. The BMMY medium was found to be optimal for the hepcidin protein expression and growth of the recombinant strains. Hepcidin protein expressed in recombinant strains was about 3 mg/L. Peptide expression was verified by Western blotting and ELISA assay. Recombinant hepc 20 was purified through Reverse-Phase HPLC column and characterized by Mass Spectrometry and amino acid sequencing. It also exhibited antibacterial activity against Staphylococcus aureus and Bacillus subtilis. Codice articolo 9783639283242
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An Optimized Expression Of Recombinant Hepcidin: Using Pichia Pastoris
Da: Revaluation Books, Exeter, Regno Unito
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Paperback. Condizione: Brand New. 136 pages. 8.66x5.91x0.31 inches. In Stock. Codice articolo __3639283244
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