Tortoise lysozyme, unlike hen lysozyme, does not distinguish between the α- and β-anomeric forms of N-acetyl D-glucosamine. This indicates that α- and β-anomeric forms of the inhibitor have the same affinities and experience identical magnetic environments in tortoise lysozyme. The dissociation constant of tortoise lysozyme—inhibitor complex was calculated from chemical shift data and found to be 3.5 × 10−2 M. The enthalpy of dissociation was calculated to be 5.0 kcal/mol.
