Abstract
1. 1. The conformations of the apoenzyme, the holoenzyme and a model of enzyme-substrate complex of d-amino acid oxidase ( d-amino acid: O 2 oxidoreductase (deaminating), EC 1.4.3.3), were determined by using β-function obtained from the combination of hydrodynamic properties, together with the results of light-scattering and of optical-rotatory-dispersion measurements. 2. 2. The results indicate that remarkable changes in conformation of the molecule (from random ellipsoid to rigid sphere) occur with the change from apoenzyme to enzyme-substrate model. 3. 3. The above changes are discussed in connection with the mechanism of the enzymic catalysis.
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