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Systematic cyanobacterial membrane proteome analysis by combining acid hydrolysis and digestive enzymes with nano-liquid chromatography-Fourier transform mass spectrometry
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2010 (English)In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1217, no 3, 285-293 p.Article in journal (Refereed) Published
Abstract [en]

The 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.

Place, publisher, year, edition, pages
2010. Vol. 1217, no 3, 285-293 p.
Keyword [en]
Acid hydrolysis/chymotrypsin, Acid hydrolysis/trypsin, Synechocystis sp PCC 6803, Trans-membrane domain, Integral membrane protein, HPLC, nano-LC-MS
National Category
Natural Sciences
URN: urn:nbn:se:su:diva-50315DOI: 10.1016/j.chroma.2009.11.045ISI: 000273912300006OAI: diva2:380756
authorCount :10Available from: 2010-12-22 Created: 2010-12-22 Last updated: 2010-12-22Bibliographically approved

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Norling, Birgitta
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Department of Biochemistry and Biophysics
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