Literature DB >> 9408163

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

J B Ghaim1, P H Tsatsos, A Katsonouri, D M Mitchell, R Salcedo-Hernandez, R B Gennis.   

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.

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Year:  1997        PMID: 9408163     DOI: 10.1016/s0005-2736(97)00127-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex.

Authors:  Nina Morgner; Thomas Kleinschroth; Hans-Dieter Barth; Bernd Ludwig; Bernhard Brutschy
Journal:  J Am Soc Mass Spectrom       Date:  2007-04-29       Impact factor: 3.109

2.  Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix.

Authors:  Yoshiki Kabashima; Junshi Sakamoto
Journal:  BMC Microbiol       Date:  2011-03-14       Impact factor: 3.605

3.  A Bacterial Stress Response Regulates Respiratory Protein Complexes To Control Envelope Stress Adaptation.

Authors:  Randi L Guest; Junshu Wang; Julia L Wong; Tracy L Raivio
Journal:  J Bacteriol       Date:  2017-09-19       Impact factor: 3.490

  3 in total

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