Abstract
1. Titration of benzylamine oxidase with benzylamine under anaerobic conditions shows that full reduction of the enzymic 470-nm chromophore is obtained on the addition of one mole of substrate per mole of enzyme. Concomitantly, one mole of benzaldehyde per mole of enzyme is produced. 2. A single prosthetic group interacting with carbonyl reagents can be detected on titration of benzylamine oxidase with phenylhydrazine. Titration data reported to indicate a higher content of prosthetic groups were obtained under conditions where equilibration between enzyme and phenylhydrazine is insufficiently complete. 3. It is concluded that pig-plasma benzylamine oxidase contains a single catalytically active site. This means that the two copper atoms present in the enzyme may be structurally or functionally different.
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