Abstract
1. 1. Lysozymes from hen, duck II and goose egg white and human lysozyme were compared at the level of their tryptophyl residues using the solvent perturbation technique and fluorescence emission in addition to two chemical modifications. 2. 2. The three tryptophyl residues of goose lysozyme were found completely exposed to the solvent. 3. 3. The study of the situation of the aromatic residues of hen, duck II and human lysozymes provided additional evidence that the three dimensional structures of these enzymes are very similar although an unexpected reactivity of tryptophan 28 of human lysozyme towards N-bromosuccinimide could be evidenced.
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