Interference by amino acids in the estimation of sugars by reductometric methods.

H. G. BRAY, K. WHITE AND P. B. WOOD I955 3. Values for four apparent dissociation constants have been determined and the magnitude of another calculated. 4. Preliminary experiments have been performed on the inhibition of n-hexanamide hydrolysis by carboxylate ions other than n-hexanoate. 5. The effect of temperature on the hydrolysis has been studied: the apparent energy of activation is 10-5 kcal. between 8-1 and 37-2°. 6. The optimumpH ofthe reaction is about 87 at 37.20: at higher pH values irreversible inactivation takes place. 7. The results are discussed in terms of the relative affinities of two groups on the catalytic site of the enzyme for substrate/or inhibitor.