Formation of dityrosine cross-links in proteins by oxidation of tyrosine residues

Abstract

1. Enzymic oxidation of proteins with peroxidase and hydrogenperoxide at a basic pH value leads to an oxidative phenolic coupling of adjacent tyrosine residues forming cross-linked proteins. 2. Dityrosine (3,3'-bityrosine) was identified as the cross-link in oxidised proteins by thin-layer chromatography, amino acid analysis and fluorescence measurements. 3. Gel filtration experiments with oxidised insulin showed that the cross-linkage is predominantly intermolecular. 4. In tetranitromethane treated proteins, dityrosine could be identified after hydrolysis.