Top down proteomics of human membrane proteins from enriched mitochondrial fractions

Adam D. Catherman, Mingxi Li, John C. Tran, Kenneth R. Durbin, Philip D. Compton, Bryan P. Early, Paul M. Thomas, Neil L. Kelleher*

*Corresponding author for this work

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

The interrogation of intact integral membrane proteins has long been a challenge for biological mass spectrometry. Here, we demonstrate the application of top down mass spectrometry to whole membrane proteins below 60 kDa with up to 8 transmembrane helices. Analysis of enriched mitochondrial membrane preparations from human cells yielded identification of 83 integral membrane proteins, along with 163 membrane-associated or soluble proteins, with a median q value of 3 × 10-10. An analysis of matching fragment ions demonstrated that significantly more fragment ions were found within transmembrane domains than would be expected based upon the observed protein sequence. In total, 46 proteins from the complexes of oxidative phosphorylation were identified which exemplifies the increasing ability of top down proteomics to provide extensive coverage in a biological network.

Original languageEnglish (US)
Pages (from-to)1880-1888
Number of pages9
JournalAnalytical Chemistry
Volume85
Issue number3
DOIs
StatePublished - Feb 5 2013

ASJC Scopus subject areas

  • Analytical Chemistry

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