Systematic cyanobacterial membrane proteome analysis by combining acid hydrolysis and digestive enzymes with nano-liquid chromatography-Fourier transform mass spectrometry

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dc.contributor.authorJ Kwon-
dc.contributor.authorJ Oh-
dc.contributor.authorC Park-
dc.contributor.authorK Cho-
dc.contributor.authorS I Kim-
dc.contributor.authorS Kim-
dc.contributor.authorSung Hoon Lee-
dc.contributor.authorJong Hwa Park-
dc.contributor.authorB Norling-
dc.contributor.authorJ S Choi-
dc.date.accessioned2017-04-19T09:17:12Z-
dc.date.available2017-04-19T09:17:12Z-
dc.date.issued2010-
dc.identifier.issn00219673-
dc.identifier.uri10.1016/j.chroma.2009.11.045ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9337-
dc.description.abstractThe identification of membrane proteins is currently under-represented since the trans-membrane domains of membrane proteins have a hydrophobic property. Membrane proteins have mainly been analyzed by cleaving and identifying exposed hydrophilic domains. We developed the membrane proteomics method for targeting integral membrane proteins by the following sequential process: in-solution acid hydrolysis, reverse phase chromatographic separation, trypsin or chymotrypsin digestion and nano-liquid chromatography-Fourier transform mass spectrometry. When we employed total membrane proteins of Synechocystis sp. PCC 6803, 155 integral membrane proteins out of a predictable 706 were identified in a single application, corresponding to 22% of a genome. The combined methods of acid hydrolysis-trypsin (AT) and acid hydrolysis-chymotrypsin (AC) identified both hydrophilic and hydrophobic domains of integral membrane proteins, respectively. The systematic approach revealed a more concrete data in mapping the repertoire of cyanobacterial membrane and membrane-linked proteome.-
dc.publisherElsevier-
dc.titleSystematic cyanobacterial membrane proteome analysis by combining acid hydrolysis and digestive enzymes with nano-liquid chromatography-Fourier transform mass spectrometry-
dc.title.alternativeSystematic cyanobacterial membrane proteome analysis by combining acid hydrolysis and digestive enzymes with nano-liquid chromatography-Fourier transform mass spectrometry-
dc.typeArticle-
dc.citation.titleJournal of Chromatography A-
dc.citation.number3-
dc.citation.endPage293-
dc.citation.startPage285-
dc.citation.volume1217-
dc.contributor.alternativeName권조셉-
dc.contributor.alternativeName오지현-
dc.contributor.alternativeName박치열-
dc.contributor.alternativeName조근-
dc.contributor.alternativeName김승일-
dc.contributor.alternativeName김수현-
dc.contributor.alternativeName이성훈-
dc.contributor.alternativeName박종화-
dc.contributor.alternativeNameNorling-
dc.contributor.alternativeName최종순-
dc.identifier.bibliographicCitationJournal of Chromatography A, vol. 1217, no. 3, pp. 285-293-
dc.identifier.doi10.1016/j.chroma.2009.11.045-
dc.subject.keywordAcid hydrolysis/chymotrypsin-
dc.subject.keywordAcid hydrolysis/trypsin-
dc.subject.keywordHPLC-
dc.subject.keywordIntegral membrane protein-
dc.subject.keywordnano-LC-MS-
dc.subject.keywordSynechocystis sp. PCC 6803-
dc.subject.keywordTrans-membrane domain-
dc.subject.localAcid hydrolysis/chymotrypsin-
dc.subject.localAcid hydrolysis/trypsin-
dc.subject.localHPLC-
dc.subject.localIntegral membrane protein-
dc.subject.localnano-LC-MS-
dc.subject.localSynechocystis sp. PCC 6803-
dc.subject.localTrans-membrane domain-
dc.subject.localTransmembrane domain-
dc.description.journalClassY-
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