Isolation protocol for two-dimensional-polyacrylamide gel electrophoresis analysis of
            <i>Haloferax volcanii</i>
            proteome

Evans, Edward C.; Horn, Troy; Wagner, Mary Ann; Eschenbrenner, Michel; Mujer, Cesar V.; DelVecchio, Vito G.

doi:10.2144/03353bm07

Cited by 4 publications

(2 citation statements)

References 7 publications

(6 reference statements)

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“…As shown in Fig. 1 , proteins were well resolved in the acidic range and very limited streaking was observed at higher MW range, unlike earlier reports [ 6 , 7 , 21 , 22 ]. However, acidic proteins which were resolved through unmodified 2-D gel procedure resulted in horizontal and vertical streaking at higher MW range.…”

Section: Resultscontrasting

confidence: 65%

“…Bioinformatic analyses of the NRC-1 genome have shown the predicted proteome to be extremely acidic, with a median pI of only 4.9 [ 2 ]. Preliminary experimental proteomic analysis of Halobacterium NRC-1 and related halophiles has exhibited the feasibility of both two-dimensional gel electrophoretic (2-DE) analysis [ 6 , 7 ], liquid chromatography coupled tandem mass spectrometry (LC-MS/MS), and MALDI-TOF analysis [ 7 , 8 ]. Furthermore, mass spectrometric analysis of purple membrane preparations from Halobacterium has also been reported [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

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Proteomic analysis of acidic chaperones, and stress proteins in extreme halophile Halobacterium NRC-1: a comparative proteomic approach to study heat shock response

Shukla

2006

Proteome Sci

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Background: Halobacterium sp. NRC-1 is an extremely halophilic archaeon and has adapted to optimal growth under conditions of extremely high salinity. Its proteome is highly acidic with a median pI of 4.9, a unique characteristic which helps the organism to adapt high saline environment. In the natural growth environment, Halobacterium NRC-1 encounters a number of stressful conditions including high temperature and intense solar radiation, oxidative and cold stress. Heat shock proteins and chaperones play indispensable roles in an organism's survival under many stress conditions. The aim of this study was to develop an improved method of 2-D gel electrophoresis with enhanced resolution of the acidic proteome, and to identify proteins with diverse cellular functions using in-gel digestion and LC-MS/MS and MALDI-TOF approach.

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