Article

 

Evaluating peroxiredoxin sensitivity towards inactivation by peroxide substrates Public Deposited

Downloadable Content

Download PDF
https://ir.library.oregonstate.edu/concern/articles/c534fp769

Descriptions

Attribute NameValues
Creator
Abstract
  • Peroxiredoxins (Prxs) are very effective peroxide reducing enzymes, but also are susceptible to being oxidatively inactivated by their own substrates. The level of sensitivity to such hyperoxidation varies depending both on the enzyme involved and the type of peroxide substrate. For some Prxs, the hyperoxidation has physiological relevance, so it is important to define approaches that can be used to quantify sensitivity. Here we describe three distinct approaches that can be used to obtain quantitative or semiquantitative estimates of Prx sensitivity and define C[subscript hyp1%] as a simple way of quantifying sensitivity so that values can easily be compared.
Resource Type
DOI
Date Available
Date Issued
Citation
  • Nelson, K. J, Parsonage, D., Karplus, P. A., & Poole, L. B. (2013). Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Methods in Enzymology 527: 21-40. doi:10.1016/B978-0-12-405882-8.00002-7
Journal Title
Journal Volume
  • 527
Academic Affiliation
Keyword
Rights Statement
Funding Statement (additional comments about funding)
  • This work was supported by U. S. Public Health Service Grant GM050389 from the National Institutes of Health and by a 2011 Spark drug discovery grant from Wake Forest School of Medicine.
Publisher
Peer Reviewed
Language
Replaces
Additional Information
  • description.provenance : Made available in DSpace on 2013-09-30T22:43:37Z (GMT). No. of bitstreams: 1 KarplusPAndrewBiochemistryBiophysicsEvaluatingPeroxiredoxinSensitivity.pdf: 686610 bytes, checksum: 8aac02e788bf44bf7b78c43ae5f11aad (MD5) Previous issue date: 2013
  • description.provenance : Approved for entry into archive by Deanne Bruner(deanne.bruner@oregonstate.edu) on 2013-09-30T22:43:37Z (GMT) No. of bitstreams: 1 KarplusPAndrewBiochemistryBiophysicsEvaluatingPeroxiredoxinSensitivity.pdf: 686610 bytes, checksum: 8aac02e788bf44bf7b78c43ae5f11aad (MD5)
  • description.provenance : Submitted by Deanne Bruner (deanne.bruner@oregonstate.edu) on 2013-09-30T22:41:51Z No. of bitstreams: 1 KarplusPAndrewBiochemistryBiophysicsEvaluatingPeroxiredoxinSensitivity.pdf: 686610 bytes, checksum: 8aac02e788bf44bf7b78c43ae5f11aad (MD5)

Relationships

Parents:

This work has no parents.

Items