The cross-linking of tyrosine residues in apo-ovotransferrin by treatment with periodate anions.
The iron-binding ability of apotransferrins is rapidly abolished in the reaction with periodate anions, which destroys 4 mol of tyrosine per mol of protein. Treatment of ovotransferrin with cyanogen bromide and tryptic digestion of the glycopeptide fragment demonstrated the existence of an intramolecular cross-link in the C-terminal domain of the oxidized protein. The cross-linked residues were identified as Tyr-421 and Tyr-524 and the product is similar in structure to 3,3'-dityrosine.
Hsuan
J J
JJ
Department of Biochemistry, University of Bristol, U.K.
D000596:Amino Acids / Q000032:analysis; D001059:Apoproteins; D001665:Binding Sites; D003207:Conalbumin; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D004527:Egg Proteins; D013058:Mass Spectrometry; D010446:Peptide Fragments / Q000032:analysis*; D010449:Peptide Mapping; D010504:Periodic Acid / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D014443:Tyrosine / Q000031:analogs & derivatives / Q000032:analysis*
D000596:Amino Acids; D001059:Apoproteins; D003432:Cross-Linking Reagents; D004527:Egg Proteins; D010446:Peptide Fragments; D010504:Periodic Acid; D003207:Conalbumin; D014443:Tyrosine; C009288:metaperiodate; C007543:dityrosine