Matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS) was used to analyze the protein composition in several common and durum wheat varieties. Mass spectra were obtained directly from crude and partially puriÐed wheat gliadin and reduced glutenin subunit fractions. Mass spectra of
Matrix Compatible Buffers for Analysis of Proteins with Matrix-assisted Laser Desorption/Ionization Mass Spectrometry
✍ Scribed by Ute Kallweit; K. Olaf Börnsen; Gerhard M. Kresbach; H. Michael Widmer
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 506 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0951-4198
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✦ Synopsis
Different buffers typically used in biological applications were evaluated for compatibility with matrix-assisted laser desorptiodionization m a s spectrometry (MALDI-MS) measurements. It was found that the buffers recommended by Good and co-workers, such as HEPES and MOPS in concentrations below 5 0 m ~ do not negatively affect the MALDI-MS measurements, a fact that is in contrast to phosphate buffers. Furthermore, increased peak intensities are observed in their presence as compared with pure water or other buffers. Additionally, buffer and salt concentrations higher than 1 0 0 m could be reduced by optimized purification methods, like drop dialysis or protein immobilization on transfer membranes.
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