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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

Authors 

J KwonJ OhC ParkK ChoS I KimS KimSung Hoon LeeJong Hwa ParkB NorlingJ S Choi

Publisher 

Elsevier

Issue Date 

2010

Citation 

Journal of Chromatography A, vol. 1217, no. 3, pp. 285-293

Keywords 

Acid hydrolysis/chymotrypsinAcid hydrolysis/trypsinHPLCIntegral membrane proteinnano-LC-MSSynechocystis sp. PCC 6803Trans-membrane domain

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.

ISSN 

0021-9673

Link 

http://dx.doi.org/10.1016/j.chroma.2009.11.045

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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