Regular ArticleExtraction Method for Analysis of Detergent-Solubilized Bacteriorhodopsin and Hydrophobic Peptides by Electrospray Ionization Mass Spectrometry☆,☆☆
References (30)
- et al.
Anal. Biochem.
(1996) - et al.
Anal. Biochem.
(1993) - et al.
Biophys. J.
(1992) - et al.
Anal. Biochem.
(1993) - et al.
Meth. Enzymol.
(1974) - et al.
J. Mol. Biol.
(1996) - et al.
J. Biol. Chem.
(1989) - et al.
Biochim. Biophys. Acta
(1993) - et al.
J. Biol. Chem.
(1998) - et al.
J. Mass Spectrometry
(1995)
Science
Rapid Commun. Mass Spectrom.
Protein Sci.
Biochem. Soc. Trans.
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Abbreviations used: MALDI, matrix-assisted laser desorption/ionization; ESI, electrospray ionization; BR, bacteriorhodopsin; CTAB, cetyltrimethylammonium bromide; OG, octyl-β-glucoside;CHAPSO, 3-(3-cholamidopropyl)dimethylammonio-2-hydroxy-1-propanesulfonate; BO, bacterioopsin.
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Simpson, C. F.Whittaker, M.
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