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The identification of disulfides in ricin D using proteolytic cleavage followed by negative-ion nano-electrospray ionization mass spectrometry of the peptide fragments.

Authors
  • Tran, T T Nha
  • Brinkworth, Craig S
  • Bowie, John H
Type
Published Article
Journal
Rapid Communications in Mass Spectrometry
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jan 30, 2015
Volume
29
Issue
2
Pages
182–190
Identifiers
DOI: 10.1002/rcm.7088
PMID: 25641493
Source
Medline
License
Unknown

Abstract

The positions of the five disulfide groups in ricin D may be determined by characteristic negative-ion cleavage of the disulfide groups, while sequence information may be determined using the standard negative-ion backbone cleavages of the resulting cleaved peptides. Negative-ion mass spectrometry can also be used to provide partial sequencing information for other peptides (i.e. those not containing Cys) using the standard negative-ion backbone cleavages of these peptides.

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