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pubmed-article:20727013pubmed:abstractTextIn this study, we describe the characterization, cloning, expression and purification of the lysin A gene of the mycobacteriophage TM4. The gene TM4_gp29 (gp29) is a 1644-bp gene that codes for a 58.6-kDa protein and contains peptidoglycan recognition protein, Zn-binding and amidase catalytic domains. The gene was cloned into Escherichia coli using the 'His-Tag' pQE60 vector. After affinity chromatography-mediated purification, the protein was concentrated and visualized using sodium dodecyl sulphate polyacrylamide gel electrophoresis. Evidence of peptidoglycan-degrading activity was observed initially by a chloroform assay and later by conventional zymogram analysis.lld:pubmed
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pubmed-article:20727013pubmed:authorpubmed-author:CoffeyAidanAlld:pubmed
pubmed-article:20727013pubmed:authorpubmed-author:BegleyMáireMlld:pubmed
pubmed-article:20727013pubmed:authorpubmed-author:NeveHorstHlld:pubmed
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pubmed-article:20727013pubmed:authorpubmed-author:RossReynolds...lld:pubmed
pubmed-article:20727013pubmed:copyrightInfo© 2010 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.lld:pubmed
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pubmed-article:20727013pubmed:volume311lld:pubmed
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pubmed-article:20727013pubmed:pagination126-32lld:pubmed
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pubmed-article:20727013pubmed:year2010lld:pubmed
pubmed-article:20727013pubmed:articleTitleCloning and expression of a mureinolytic enzyme from the mycobacteriophage TM4.lld:pubmed
pubmed-article:20727013pubmed:affiliationDepartment of Biological Sciences, Cork Institute of Technology, Cork, Ireland.lld:pubmed
pubmed-article:20727013pubmed:publicationTypeJournal Articlelld:pubmed
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