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

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Title
Systematic cyanobacterial membrane proteome analysis by combining acid hydrolysis and digestive enzymes with nano-liquid chromatography-Fourier transform mass spectrometry
Author(s)
J Kwon; J Oh; C Park; K Cho; S I Kim; S Kim; Sung Hoon Lee; Jong Hwa Park; B Norling; J S Choi
Bibliographic Citation
Journal of Chromatography A, vol. 1217, no. 3, pp. 285-293
Publication Year
2010
Abstract
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.
Keyword
Acid hydrolysis/chymotrypsinAcid hydrolysis/trypsinHPLCIntegral membrane proteinnano-LC-MSSynechocystis sp. PCC 6803Trans-membrane domain
ISSN
0021-9673
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.chroma.2009.11.045
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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