Studies on the Mode of Enzyme Catalysis and the Hydrolysis of Bis-P-Dimethylaminobenzalazine

Citation

Lutwack, Ralph (1955) Studies on the Mode of Enzyme Catalysis and the Hydrolysis of Bis-P-Dimethylaminobenzalazine. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/CA38-8B92. https://resolver.caltech.edu/CaltechETD:etd-01262004-093505

Abstract

The alpha-chymotrypsin catalyzed hydrolysis of four L-tyrosinhydrazides at 25[degrees]C have been studied. The values of the kinetic constants K[subscript s] and k[subscript 3] for L-tyrosinhydrazide, acetyl L-tyrosinhydrazide, and nicotinyl L-tyrosinhydrazide have been evaluated by the usual procedure. The values of these constants for benzoyl L-tyrosinhydrazide have been obtained by the method of competitive hydrolysis. The procedure for the quantitative determination of hydrazine by the reaction with p-dimethylaminobenzaldehyde to form the corresponding azine has been adapted to the study of the rate of the hydrolysis of alpha-amino acid hydrazides. The rates of formation and of hydrolysis of bis p-dimethylaminobenzalazine have been studied under various conditions. The effects of dielectric constant, ionic strength, acid concentration, and temperature on the rate of hydrolysis have been investigated. The acid dissociation constants for p-dimethylaminobenzaldehyde in two distinct ethanol-water systems have been determined. The acid dissociation constants for the hydrazone and the azine of p-dimethylaminobenzaldehyde have been obtained. The value of the constant for the assumed aldehyde- hydrazine- hydrazone equilibrium has been calculated.

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