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Article: A monobromoacetate dehalogenase from Pseudomonas cepacia MBA4

TitleA monobromoacetate dehalogenase from Pseudomonas cepacia MBA4
Authors
KeywordsDehalogenase
Monobromoacetic Acid
Purification
Issue Date1988
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00203/index.htm
Citation
Archives Of Microbiology, 1988, v. 150 n. 5, p. 441-446 How to Cite?
AbstractPseudomonas cepacia MBA4 able to utilize monobromoacetic acid as a sole source of carbon and energy was isolated from soil by enrichment culture. In batch culture the ability to utilize the substrate was conferred by a single halidohydrolase-type dehalogenase which demonstrated a high activity towards the enrichment substrate. The purified enzyme, designated as dehalogenase IVa by activity-stain polyacrylamide gel electrophoresis, had a relative molecular weight of 45,000 and was comprised of two electrophoretically identical subunits with relative molecular weights of 23,000. Dehalogenase IVa demonstrated isomer specificity, being active towards the L-isomer of 2-monochloropropionic acid only. The significance of activity-stain polyacrylamide gel electrophoresis in characterizing dehalogenases and their ubiquitous distribution among bacterial genera are discussed. © 1988 Springer-Verlag.
Persistent Identifierhttp://hdl.handle.net/10722/178363
ISSN
2015 Impact Factor: 1.76
2015 SCImago Journal Rankings: 0.702
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTsang, JSHen_US
dc.contributor.authorSallis, PJen_US
dc.contributor.authorBull, ATen_US
dc.contributor.authorHardman, DJen_US
dc.date.accessioned2012-12-19T09:47:16Z-
dc.date.available2012-12-19T09:47:16Z-
dc.date.issued1988en_US
dc.identifier.citationArchives Of Microbiology, 1988, v. 150 n. 5, p. 441-446en_US
dc.identifier.issn0302-8933en_US
dc.identifier.urihttp://hdl.handle.net/10722/178363-
dc.description.abstractPseudomonas cepacia MBA4 able to utilize monobromoacetic acid as a sole source of carbon and energy was isolated from soil by enrichment culture. In batch culture the ability to utilize the substrate was conferred by a single halidohydrolase-type dehalogenase which demonstrated a high activity towards the enrichment substrate. The purified enzyme, designated as dehalogenase IVa by activity-stain polyacrylamide gel electrophoresis, had a relative molecular weight of 45,000 and was comprised of two electrophoretically identical subunits with relative molecular weights of 23,000. Dehalogenase IVa demonstrated isomer specificity, being active towards the L-isomer of 2-monochloropropionic acid only. The significance of activity-stain polyacrylamide gel electrophoresis in characterizing dehalogenases and their ubiquitous distribution among bacterial genera are discussed. © 1988 Springer-Verlag.en_US
dc.languageengen_US
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00203/index.htmen_US
dc.relation.ispartofArchives of Microbiologyen_US
dc.subjectDehalogenaseen_US
dc.subjectMonobromoacetic Aciden_US
dc.subjectPurificationen_US
dc.titleA monobromoacetate dehalogenase from Pseudomonas cepacia MBA4en_US
dc.typeArticleen_US
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_US
dc.identifier.authorityTsang, JSH=rp00792en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/BF00422284en_US
dc.identifier.scopuseid_2-s2.0-0000560575en_US
dc.identifier.volume150en_US
dc.identifier.issue5en_US
dc.identifier.spage441en_US
dc.identifier.epage446en_US
dc.identifier.isiWOS:A1988Q002900006-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridTsang, JSH=7102483508en_US
dc.identifier.scopusauthoridSallis, PJ=36920491900en_US
dc.identifier.scopusauthoridBull, AT=24538530400en_US
dc.identifier.scopusauthoridHardman, DJ=7004649669en_US

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