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
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Cytochrome b Group
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Cytochromes / chemistry*
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Electron Transport Chain Complex Proteins*
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Electron Transport Complex III / chemistry
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Electron Transport Complex IV / chemistry
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / chemistry
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Escherichia coli / enzymology
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Escherichia coli Proteins*
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Membrane Proteins / chemistry*
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Membrane Proteins / isolation & purification
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Molecular Weight*
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Oxidoreductases / chemistry*
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Protein Conformation
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Rhodobacter sphaeroides / chemistry
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Rhodobacter sphaeroides / enzymology
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization*
Substances
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Cytochrome b Group
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Cytochromes
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Electron Transport Chain Complex Proteins
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Escherichia coli Proteins
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Membrane Proteins
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cytochrome bo3, E coli
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Oxidoreductases
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cytochrome bd terminal oxidase complex, E coli
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Electron Transport Complex IV
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Electron Transport Complex III