Practical Protein Chemistry - A. Darbre 1989

Chemical fragmentation of polypeptides
Cleavage at tyrosine residues
Other reagents

N-Iodosuccinimide is just as effective as N-Bromosuccinimide in the oxidative Cleavage reaction of the Tyrosine peptide bond. The reaction is carried out at pH 4.5, with yields ranging from 25–95% for model compounds and simple tyrosine-containing Peptides. The reaction mechanism is identical to the cleavage induced by N-bromosuccinimide [100]. It has been shown that the tyrosine peptide bond is cleaved with a moderate yield upon electrolytic oxidation at a platinum electrode. Unlike the reaction with N-bromosuccinimide, no Cleavage at Tryptophan and Histidine residues is observed; however, oxidation of other functional groups (imidazole, thioether, disulfide, and amino groups) does occur, albeit at a slower rate than that of the phenolic groups of tyrosine. Using this method, angiotensin, Insulin, and Ribonuclease were specifically fragmented at the tyrosine residue [30].



Last update: 06/08/2026

Editorial and Educational Adaptation: This material has been compiled based on the primary/original source text. The project team performed an editorial review, corrected technical inaccuracies, structured sections, and adapted the content for an educational format.

What was processed:

  • elimination of formatting defects (OCR errors, structural breaks, corrupted characters);
  • editorial organization of content;
  • standardization of terminology in accordance with academic sources;
  • verification of factual statements against the original source text.

All mentions of the author, publication year, and origin of the primary text have been preserved in accordance with the source.