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Differential isotopic mass splitting as a mass spectrometric tool for identifying protease substrates
- Source :
- Rapid Communications in Mass Spectrometry. 16:1054-1058
- Publication Year :
- 2002
- Publisher :
- Wiley, 2002.
-
Abstract
- A method is described whereby stable isotopic signatures were partially incorporated into both termini of a peptide sequence giving rise to a characteristic cluster of four peaks in the mass spectral analysis. Cleavage of this peptide by a protease between the labeled positions generates two fragments both displaying their own individual signature peaks. The event of protease cleavage of the peptide was monitored by the changes in clusters within the spectrum. We believe that this technique could be used to aid the discovery of new cleavage substrates for proteases. Additionally, the analysis can be automated with dedicated software designed to select and interpret the data since all peaks of interest contain predefined signatures and can be easily distinguished from background noise. Copyright © 2002 John Wiley & Sons, Ltd.
- Subjects :
- chemistry.chemical_classification
Proteases
Protease
Stereochemistry
Chemistry
medicine.medical_treatment
Organic Chemistry
Peptide
Mass spectrometric
Combinatorial chemistry
Mass Spectrometry
Substrate Specificity
Analytical Chemistry
Sequence Analysis, Protein
Isotope Labeling
medicine
Cluster (physics)
Neprilysin
Trypsin
Spectral analysis
Peptides
Peptide sequence
Chromatography, High Pressure Liquid
Software
Spectroscopy
Subjects
Details
- ISSN :
- 10970231 and 09514198
- Volume :
- 16
- Database :
- OpenAIRE
- Journal :
- Rapid Communications in Mass Spectrometry
- Accession number :
- edsair.doi.dedup.....afe1d076c40d2637b731e9e536783e01