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  • Title: Oxidation of tryptophan in lysozyme by ozone in aqueous solution.
    Author: Kuroda M, Sakiyama F, Narita K.
    Journal: J Biochem; 1975 Oct; 78(4):641-51. PubMed ID: 1213983.
    Abstract:
    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 located in position 62 (or 63) of the protein.
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