Oxidation of tryptophan in lysozyme by ozone in aqueous solution.

@article{Kuroda1975OxidationOT,
  title={Oxidation of tryptophan in lysozyme by ozone in aqueous solution.},
  author={Makoto Kuroda and Fumio Sakiyama and K Narita},
  journal={Journal of biochemistry},
  year={1975},
  volume={78 4},
  pages={641-51}
}
A tryptophan residue in hen's egg-white lysozyme [EC 3.2.1.17] was modified by ozone in an aqueous solution. One of the six tryptophan residues in the enzyme was oxidized to N'-formylkynurenine with concomitant loss of the enzymatic activity. Physicochemical studies of this modified enzyme (OL-I) revealed that the ozonization of lysozyme in aqueous media resulted in little change of the gross molecular conformation. It was deduced that the modified tryptophan residue in OL-I was possibly… CONTINUE READING