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Quantification of Membrane Proteins Using Nonspecific Protease Digestions

  • Maria Bendz
  • Mirja Carlsson Möller
  • Giorgio Arrigoni
  • Åsa Wåhlander
  • Roberto Stella
  • Salvatore Cappadona
  • Fredrik Levander
  • Lars Hederstedt
  • Peter James
Publishing year: 2009
Language: English
Pages: 5666-5673
Publication/Series: Journal of Proteome Research
Volume: 8
Issue: 12
Document type: Journal article
Publisher: The American Chemical Society

Abstract english

We present a mass spectrometry-based method for the identification and quantification of membrane proteins using the low-specificity protease Proteinase K, at very high pH, to digest proteins isolated by a modified SDS-PAGE protocol. The resulting peptides are modified with a fragmentation-directing isotope labeled tag. We apply the method to quantify differences in membrane protein expression of Bacillus subtilis grown in the presence or absence of glucose.


  • Immunology in the medical area
  • membrane proteins
  • N-terminal labeling
  • quantification
  • relative
  • proteinase K
  • Bacillus subtilis


  • ISSN: 1535-3893
Peter James
E-mail: peter [dot] james [at] immun [dot] lth [dot] se


Department of Immunotechnology

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