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Suppression of matrix clusters and enhancement of peptide signals in MALDI-TOF mass spectrometry using nitrilotriacetic acid
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Web of Science
Cited 20 time in Scopus
- Authors
- Issue Date
- 2005-11
- Publisher
- American Chemical Society
- Citation
- Analytical Chemistry, Vol.77 No.22, pp.7483-7488
- Abstract
- Matrix clusters and their alkali metal ion adducts suppress peptide signals in the 500-1400 Da range and compromise MALDI-TOF mass spectrometric peptide mass fingerprinting and protein identification. Addition of 7 mM nitrilotriacetic acid to the matrix solution significantly reduced matrix clusters and increased signal-to-noise ratio of peptide signals similar to 5 to 20-fold. As a result, reliability in the identification of femtomole amounts of proteins based on peptide mass fingerprinting and database search was significantly enhanced, leading to a higher score and sequence coverage.
- ISSN
- 0003-2700
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