A number of different procedures have been developed for use with matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS) for the analysis of non-covalent protein-protein complexes. These include use of specific matrix and laser combinations, accumulation of "first shot" spectra, mo
Picoliter to nanoliter deposition of peptide and protein solutions for matrix-assisted laser desorption/ionization mass spectrometry
β Scribed by G. Allmaier
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 77 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0951-4198
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Two copper proteins azurin-1 and azurin-2 were isolated from denitrifying bacteria Alcaligenes xylosoxidans GIFU1051, and the mass spectrometric analysis of the proteins were carried out by both matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) and electrospray ionization (ESI).
Transition metal ion complexes with proteins and peptides are important in many areas of analytical and biological chemistry. We used positive and negative ion MALDI-MS to detect complexes with Cu and Ni ions, and show that the speciΓc and non-speciΓc transition metal ion-peptide complexes can be di
The analysis of oligonucleotides using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has led to the investigation of the use of matrix additives (i.e., co-matrices) to help improve the poor spectral quality commonly observed during the analysis of this class of compounds.