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Multiple proteases to localize oxidation sites

Gu, L and Robinson, RAS (2015) Multiple proteases to localize oxidation sites. PLoS ONE, 10 (3).

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Abstract

© 2015 Gu, Robinson. Proteins present in cellular environments with high levels of reactive oxygen and nitrogen species and/or low levels of antioxidants are highly susceptible to oxidative post-translational modification (PTM). Irreversible oxidative PTMs can generate a complex distribution of modified protein molecules, recently termed as proteoforms. Using ubiquitin as a model system, we mapped oxidative modification sites using trypsin, Lys-C, and Glu-C peptides. Several M+16 Da proteoforms were detected as well as proteoforms that include other previously unidentified oxidative modifications. This work highlights the use of multiple protease digestions to give insights to the complexity of oxidative modifications possible in bottom-up analyses.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Gu, Llig32@pitt.eduLIG32
Robinson, RAS
Contributors:
ContributionContributors NameEmailPitt UsernameORCID
EditorAriga, HiroyoshiUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Date: 16 March 2015
Date Type: Publication
Journal or Publication Title: PLoS ONE
Volume: 10
Number: 3
DOI or Unique Handle: 10.1371/journal.pone.0116606
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
PubMed ID: 25775238
Date Deposited: 12 May 2015 19:53
Last Modified: 04 Feb 2019 16:55
URI: http://d-scholarship.pitt.edu/id/eprint/24104

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