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Biochemistry. 2000 Apr 18;39(15):4237-42.

Proteomics on full-length membrane proteins using mass spectrometry.

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1
Howard Hughes Medical Institute, Departments of Physiology and of Microbiology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles 90095, USA. lecoutre@hhmi.ucla.edu

Abstract

A general technique has been developed that allows rapid mass spectrometric analysis of full-length membrane proteins [Whitelegge, J. P., le Coutre, J., et al. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 10695-10698]. Using in-line HPLC electrospray ionization mass spectrometry (LC-MS), different native and recombinant bacterial membrane proteins of up to 61 kDa are characterized. Mass spectrometric data of four entirely different membrane proteins from three bacterial organisms, two transporters, a channel, and a porin protein are presented. In addition to determination of the molecular mass with an accuracy of +/-0.01%, the technique monitors alkylation or oxidation of single Cys residues and errors in deduced amino acid sequences. Finally, using in-line LC-MS, unknown proteins can be identified from solubilized Escherichia coli membranes without prior purification.

PMID:
10757971
DOI:
10.1021/bi000150m
[Indexed for MEDLINE]

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