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Updated: Aug 15, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
Published on: July 27, 2016
Ozone-induced formation of O,O'-dityrosine cross-linked in proteins
Abstract:
Treatment of spectrin, insulin, glucagon and ribonuclease with ozone results in covalent cross-linking of these proteins. This cross-linking is not reversed by treatment with dithiothreitol and thus can not be ascribed to -S-S- bond formation. A concomitant O,O'-dityrosine formation is observed by spectrofluorometric analysis of the protein and by amino acid analysis and thin-layer chromatography of hydrolyzed protein samples. It is highly probable that the observed protein cross-linking should be attributed to interpeptide O,O'-dityrosine bonds. Several authors have shown before that oxidation of proteins with horseradish peroxidase and H2O2 also leads to O,O'-dityrosine formation. Peroxidase-induced O,O'-dityrosine formation in galactose oxidase (d-galactose:oxygen 6-oxidoreductase, EC 1.1.3.9) causes a strong increase of enzyme activity. In accordance with these observations ozone treatment of galactose oxidase also leads to O,O'-dityrosine formation with a concomitant 8-fold increase of enzyme activity.
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