Proteomic investigation of natural killer cell microsomes using gas-phase fractionation by mass spectrometry

Biochim Biophys Acta. 2004 Apr 8;1698(1):87-95. doi: 10.1016/j.bbapap.2003.10.009.

Abstract

We have explored the utility of gas-phase fractionation by mass spectrometry (MS) in the mass-to-charge (m/z) dimension (GPF(m/z)) for increasing the effective number of protein identifications in cases where sample quantity limits the use of multi-dimensional chromatographic fractionation. A peptide digestate from proteins isolated from the membrane fraction of natural killer (NK) cells was analyzed by microcapillary reversed-phase liquid chromatography coupled online to an ion-trap (IT) mass spectrometer. Performing GPF(m/z) using eight narrow precursor ion scan m/z ranges enabled the identification of 340 NK cell proteins from 12 microg of digestate, representing more than a fivefold increase in the number of proteins identified as compared to the same experiment employing a standard precursor ion survey scan m/z range (i.e., m/z 400-2000). The results show that GPF(m/z) represents an effective technique for increasing protein identifications in global proteomic investigations especially when sample quantity is limited.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cation Transport Proteins / chemistry
  • Cation Transport Proteins / genetics
  • Cation Transport Proteins / metabolism
  • Killer Cells, Natural / chemistry
  • Killer Cells, Natural / metabolism*
  • Mass Spectrometry
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Mice
  • Microsomes / chemistry
  • Microsomes / metabolism*
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism
  • Proteome / chemistry
  • Proteome / metabolism*

Substances

  • Cation Transport Proteins
  • Membrane Proteins
  • Peptides
  • Proteome
  • Sfxn1 protein, mouse