Matrix-assisted laser desorption ionization mass spectrometry of membrane proteins: Demonstration of a simple method to determine subunit molecular weights of hydrophobic subunits

Joshua B. Ghaim, Panagiota H. Tsatsos, Andromachi Katsonouri, David M. Mitchell, Ruben Salcedo-Hernandez, Robert B. Gennis

Research output: Contribution to journalArticle


Matrix-assisted laser desorption ionization (MALDI) mass spectrometry has been used to obtain accurate molecular weight information for each subunit of several hydrophobic integral membrane proteins: cytochrome bo3 (4 subunits) and cytochrome bd (2 subunits) from E. coli, and the bc1 complex (3 subunits) and the cytochrome c oxidase (3 subunits) from Rhodobacter sphaeroides. The results demonstrate that the MALDI method is a convenient, quick, sensitive and reliable means for obtaining the molecular masses of the subunits of purified multisubunit membrane proteins.

Original languageEnglish (US)
Pages (from-to)113-120
Number of pages8
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number2
StatePublished - Dec 4 1997



  • Hydrophobic
  • Molecular mass
  • Protein

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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