Free radical reactions of peroxidizing lipids with amino acids and proteins: An ESR study

Karen M. Schaich, Marcus Karel

Research output: Contribution to journalArticle

88 Scopus citations

Abstract

Free radical transfer from oxidizing methyl linoleate to amino acids and proteins was studied in dry model systems incubated for periods up to 20 days. Electron spin resonance was used to study free radical production. Free radicals were detectable in the amino acids lysine, arginine, histidine, tryptophan, and cysteine. Reduced glutathione and, to a limited extent, cystine also gave free radical signals. Free radicals produced in proteins primarily showed central singlet lines, attributable to carbon-centered radicals, with g=2.004±0.001. Sulfhydryl proteins also exhibited downfield shoulders at g≄2.015 and 2.023 that were essentially identical to peaks observed in cysteine and reduced glutathione. The field positions of sulfur resonance in cysteine and proteins suggested a sulfur-oxygen complex rather than thiyl radicals.

Original languageEnglish (US)
Pages (from-to)392-400
Number of pages9
JournalLipids
Volume11
Issue number5
DOIs
Publication statusPublished - May 1 1976
Externally publishedYes

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Organic Chemistry
  • Cell Biology

Cite this