Residual EDTA bound by lens crystallins accounts for their reported resistance to copper-catalyzed oxidative damage

Xiao Lan Cui, Chuan Qin, J. Samuel Zigler

Research output: Contribution to journalArticlepeer-review

Abstract

It was recently reported that the structural proteins of the lens, the crystallins, possess unusual resistance to oxidative damage from a copper-catalyzed Fenton system. Data presented here demonstrate that this phenomenon is specific to copper-catalyzed systems and is not observed when iron is the metal catalyst. Further investigation has revealed that the apparent resistance to copper-catalyzed oxidation results from the presence of residual EDTA associated with the proteins. EDTA chelates the copper, inactivating it as a redox catalyst. This binding of EDTA to crystallins (or other proteins) occurs when the proteins present in EDTA-containing buffers are dialyzed directly against deionized water. Partial characterization of the association between EDTA and proteins is presented and its potential significance as a confounding factor in studies of the effects of metal-catalyzed oxidation on proteins is discussed.

Original languageEnglish (US)
Pages (from-to)207-213
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume308
Issue number1
DOIs
StatePublished - 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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