Presence of dityrosine bridges in thyroglobulin and their relationship with iodination

Biochem Biophys Res Commun. 1994 Jul 15;202(1):38-43. doi: 10.1006/bbrc.1994.1890.

Abstract

The presence of dimeric thyroglobulin (19S), after reduction and alkylation, suggests that within thyroglobulin there may be intermolecular cross-links, other than disulphide bridges. However, the nature of these intermolecular cross-links is still unknown. In this study, we show the presence of 3-3' dityrosine bridges in the molecule of bovine thyroglobulin by NMR and fluorescence studies. Also, we evaluated the role of iodination in dityrosine formation in vivo and in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Cell Line
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Chromatography, Liquid
  • Disulfides / analysis
  • Electrophoresis, Polyacrylamide Gel
  • Magnetic Resonance Spectroscopy
  • Propylthiouracil / pharmacology
  • Thyroglobulin / biosynthesis
  • Thyroglobulin / chemistry*
  • Thyroglobulin / isolation & purification
  • Thyroid Gland / chemistry
  • Thyroid Gland / drug effects
  • Thyroid Gland / metabolism
  • Tyrosine / analogs & derivatives*
  • Tyrosine / analysis

Substances

  • Disulfides
  • Tyrosine
  • Propylthiouracil
  • Thyroglobulin
  • dityrosine