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dc.contributor.authorPhanuphong Chaiwuten_US
dc.contributor.authorPawinee Kanasawuden_US
dc.contributor.authorPeter J. Hallingen_US
dc.date.accessioned2018-09-10T04:01:15Z-
dc.date.available2018-09-10T04:01:15Z-
dc.date.issued2007-03-05en_US
dc.identifier.issn01410229en_US
dc.identifier.other2-s2.0-33847354740en_US
dc.identifier.other10.1016/j.enzmictec.2006.07.042en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33847354740&origin=inwarden_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/60913-
dc.description.abstractGlycyl endopeptidase catalysed solid-to-solid synthesis can be carried out efficiently for the model peptides Z-Gly-Phe-NH2, Z-Gly-Leu-NH2, Z-Gly-Tyr-NH2and Z-Gly-Tyr-OEt. A small excess of acyl donor Z-Gly improved both the initial rate and final yield, whereas an excess of nucleophile Phe-NH2prevented reaction. The highest conversion was achieved when using a substrate molar ratio (Z-Gly:Phe-NH2) of 2:1. Including solid cysteine in the reaction mixture improved both initial rate and final conversion, probably by protecting the enzyme from oxidation. The reasons why conversion to Z-Gly-Phe-NH2stopped at around 83% were investigated. Entrapment of residual solid starting material did not seem significant, while autolysis and inactivation of glycyl endopeptidase in the reaction mixture during catalysis was important. The role of chemical equilibrium position was less clear. © 2006 Elsevier Inc. All rights reserved.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleSolid-to-solid peptide synthesis by glycyl endopeptidaseen_US
dc.typeJournalen_US
article.title.sourcetitleEnzyme and Microbial Technologyen_US
article.volume40en_US
article.stream.affiliationsChiang Mai Universityen_US
article.stream.affiliationsUniversity of Strathclydeen_US
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