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

Biochim Biophys Acta. 1997 Dec 4;1330(2):113-20. doi: 10.1016/s0005-2736(97)00127-2.

Abstract

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.

MeSH terms

  • Cytochrome b Group
  • Cytochromes / chemistry*
  • Electron Transport Chain Complex Proteins*
  • Electron Transport Complex III / chemistry
  • Electron Transport Complex IV / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / chemistry
  • Escherichia coli / enzymology
  • Escherichia coli Proteins*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / isolation & purification
  • Molecular Weight*
  • Oxidoreductases / chemistry*
  • Protein Conformation
  • Rhodobacter sphaeroides / chemistry
  • Rhodobacter sphaeroides / enzymology
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization*

Substances

  • Cytochrome b Group
  • Cytochromes
  • Electron Transport Chain Complex Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • cytochrome bo3, E coli
  • Oxidoreductases
  • cytochrome bd terminal oxidase complex, E coli
  • Electron Transport Complex IV
  • Electron Transport Complex III