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

• Published in: Biochimica et biophysica acta Vol. 1330; no. 2; pp. 113 - 120
• Main Authors: Ghaim, Joshua B., Tsatsos, Panagiota H., Katsonouri, Andromachi, Mitchell, David M., Salcedo-Hernandez, Ruben, Gennis, Robert B.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 04.12.1997
• Subjects: 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; Hydrophobic; MALDI; Membrane Proteins - chemistry; Membrane Proteins - isolation & purification; Molecular mass; Molecular Weight; Oxidoreductases - chemistry; Protein; Protein Conformation; Rhodobacter sphaeroides - chemistry; Rhodobacter sphaeroides - enzymology; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Molecular mass; MALDI; Protein; Hydrophobic
• ISSN: 0005-2736; 0006-3002; 1879-2642
• DOI: 10.1016/S0005-2736(97)00127-2

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 bo 3 (4 subunits) and cytochrome bd (2 subunits) from E. coli, and the be 1 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.