File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Proteomic analysis of Burkholderia cepacia MBA4 in the degradation of monochloroacetate

TitleProteomic analysis of Burkholderia cepacia MBA4 in the degradation of monochloroacetate
Authors
KeywordsBurkholderia cepacia
Haloacid
Monochloroacetate
Tandem mass spectrometry
Two-dimensional gel electrophoresis
Issue Date2007
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics
Citation
Proteomics, 2007, v. 7 n. 7, p. 1107-1116 How to Cite?
AbstractBurkholderia cepacia MBA4 is a bacterium that degrades 2-haloacids by removing the halogen and subsequent metabolism of the product for energy. In this study, 2-DE, MS/MS, and N-terminal amino acid sequencing were used to investigate the protein expression profiles of MBA4 grown in a 2-haloacid (monochloroacetate, MCA) and in the corresponding metabolic product (glycolate). Glycolate was used as a control to eliminate the proteins induced by it. Five proteins were found to be up-regulated and five proteins were down-regulated in response to MCA. The differentially expressed proteins were examined, seven of them were identified by MS/MS and two of them were sequenced by Edman degradation. Our results definitely provide an insight for understanding the physiology of B. cepacia MBA4 in response to organohalide contaminated site. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.
Persistent Identifierhttp://hdl.handle.net/10722/68434
ISSN
2021 Impact Factor: 5.393
2020 SCImago Journal Rankings: 1.260
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKwok, SYen_HK
dc.contributor.authorSiu, AFMen_HK
dc.contributor.authorNgai, SMen_HK
dc.contributor.authorChe, CMen_HK
dc.contributor.authorTsang, JSHen_HK
dc.date.accessioned2010-09-06T06:04:35Z-
dc.date.available2010-09-06T06:04:35Z-
dc.date.issued2007en_HK
dc.identifier.citationProteomics, 2007, v. 7 n. 7, p. 1107-1116en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68434-
dc.description.abstractBurkholderia cepacia MBA4 is a bacterium that degrades 2-haloacids by removing the halogen and subsequent metabolism of the product for energy. In this study, 2-DE, MS/MS, and N-terminal amino acid sequencing were used to investigate the protein expression profiles of MBA4 grown in a 2-haloacid (monochloroacetate, MCA) and in the corresponding metabolic product (glycolate). Glycolate was used as a control to eliminate the proteins induced by it. Five proteins were found to be up-regulated and five proteins were down-regulated in response to MCA. The differentially expressed proteins were examined, seven of them were identified by MS/MS and two of them were sequenced by Edman degradation. Our results definitely provide an insight for understanding the physiology of B. cepacia MBA4 in response to organohalide contaminated site. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.en_HK
dc.languageengen_HK
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomicsen_HK
dc.relation.ispartofProteomicsen_HK
dc.subjectBurkholderia cepaciaen_HK
dc.subjectHaloaciden_HK
dc.subjectMonochloroacetateen_HK
dc.subjectTandem mass spectrometryen_HK
dc.subjectTwo-dimensional gel electrophoresisen_HK
dc.titleProteomic analysis of Burkholderia cepacia MBA4 in the degradation of monochloroacetateen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=7&spage=1107&epage=1116&date=2007&atitle=Proteomic+analysis+of+Burkholderia+cepacia+MBA4+in+the+degradation+of+monochloroacetateen_HK
dc.identifier.emailSiu, AFM: fmsiu@hku.hken_HK
dc.identifier.emailChe, CM: cmche@hku.hken_HK
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_HK
dc.identifier.authoritySiu, AFM=rp00776en_HK
dc.identifier.authorityChe, CM=rp00670en_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/pmic.200600660en_HK
dc.identifier.pmid17352424-
dc.identifier.scopuseid_2-s2.0-34247547440en_HK
dc.identifier.hkuros127425en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34247547440&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume7en_HK
dc.identifier.issue7en_HK
dc.identifier.spage1107en_HK
dc.identifier.epage1116en_HK
dc.identifier.isiWOS:000245739100009-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridKwok, SY=35983108500en_HK
dc.identifier.scopusauthoridSiu, AFM=6701518489en_HK
dc.identifier.scopusauthoridNgai, SM=7006074219en_HK
dc.identifier.scopusauthoridChe, CM=7102442791en_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK
dc.identifier.issnl1615-9853-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats