The kinetics of the alpha-chymotrypsin catalyzed hydrolysis of acetyl-L-hexahydrophenylalaninamide. The influence of pH on the kinetic constants for alpha-chymotrypsin catalyzed reaction involving selected substrates and inhibitors. Genetic studies in Neurospora crassa

by Jennings, Robert R.

Abstract (Summary)
NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document. The kinetic constants for the alpha-chymotrypsin-catalyzed hydrolysis of acetyl-L-hexahydrophenylalaninamide have been determined at 25[degrees] and pH 7.9. This study indicates that aromaticity in the amino acid side chain is neither essential nor particularly helpful to the action of alpha-chymotrypsin. Some computational procedures are discussed. The kinetic constants for the alpha-chymotrypsin-catalyzed hydrolyses of L-tyrosinhydroxamide and acetyl-L-tyrosinhydroxamide have been determined at 25[degrees] at several pH's. The inhibition constants of variously ionizing inhibitors have also been determined at several pH's. The observations are generally consistent with formulations based on the existence of differently protonated forms of the enzyme and enzyme-substrate complexes. Potentiometric titrations of sour hydroxamic acids reveal that the [...] values for these acids range from 9.0 to 9.5, and that these acids are mach weaker than previously believed. Some of the conditions necessary for the good expression of the phenotype dotted in Neurospora crassa have been determined. The linkage and centromere distance of the gene controlling tyrosinase thermostability in Neurospora crassa have been determined by genetic studies.
Bibliographical Information:

Advisor:Carl Niemann

School:California Institute of Technology

School Location:USA - California

Source Type:Master's Thesis



Date of Publication:01/01/1955

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