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Peptide synthesis by recombinant Fasciola hepatica cathepsin L1

Ruth, Deborah M. and McMahon, Gillian and Ó'Fágáin, Ciarán (2006) Peptide synthesis by recombinant Fasciola hepatica cathepsin L1. Biochimie, 88 (1). pp. 117-120. ISSN 0300-9084

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Abstract

Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0–12.5% v/v acetonitrile at 37 °C. LC–MS detection indicated tripeptide formation after 10 min, continuing up to 5.5 h. The ester Z-Phe-Arg-OMe was detected throughout the experiment but the hydrolysis product Z-Phe-Arg-OH appeared early and in quite large amounts. We believe that this is the first application of a parasite protease in enzymatic peptide synthesis.

Item Type:Article (Published)
Refereed:Yes
Uncontrolled Keywords:fasciola hepatica cathepsin L1; recombinant; enzymatic peptide synthesis; cysteine proteinase;
Subjects:Biological Sciences > Biochemistry
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Chemical Sciences
DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Research Initiatives and Centres > National Centre for Sensor Research (NCSR)
Publisher:Elsevier
Official URL:http://dx.doi.org/10.1016/j.biochi.2005.06.004
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 License. View License
ID Code:78
Deposited On:26 Jun 2007 by DORAS Administrator. Last Modified 30 Jan 2009 14:08

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