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EMULSIN GLUCOSIDASE AND GALACTOSIDASE 335 3. No separation of the two activities was achieved by ammonium sulphate fractionation or by partial heat inactivation. 4. D-Glucose, D-galactose, D-glucono-1-+4-lactone and D-galactono.l-+4-lactone were competitive inhibitors with similar Ki values when measured against the two substrates. 5. Mixed substrate experiments supported the conclusion that one enzyme site is responsible for both activities. We gratefully acknowledge grants from the Research Fund of the University of London and the Nuffield Foundation.

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