Applewhite, Thomas Hood (1956) I. Thiocarbamate studies. II. Preliminary investigations of the alpha-chymotrypsin catalyzed hydrolysis of acylated amino acid esters. III. The alpha-chymotrypsin catalyzed hydrolysis of methyl hippurate and of benzoyl-L-valine methyl ester. IV. The enzyme inhibitor dissociation constants of some N-acetyl amino acid N'-methylamides. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-07082004-132616
The known reactions of N,S-diphenylthiocarbamate were extended by studies of the effects of various reagents and conditions. The results are discussed in terms of previously suggested reaction mechanisms.
The mixed anhydrides between S-phenylthiocarbonylchloride and carboxylic acids were briefly investigated as preparative intermediates. Low yields of the expected products offset the utility of this method.
The non-reactivity of secondary amine S-phenylthiocarbamates was further demonstrated with N-pentamethylene-S-phenylthiocarbamate. The inert nature of this compound indicates that the effects are not due to steric hindrance.
A brief investigation of the reactions of S-benzylthio- and 0-benzyl-N-phenylcarbamate suggest that they have little value as preparative intermediates as compared to the S- and 0-phenyl derivatives.
Some S-phenylthiocarbamates of amino acid derivatives were prepared, and their use in a polymerization reaction and stepwise dipeptide synthesis is described. The results suggest that the various methods are not as elegant as indicated earlier.
A recently developed automatic titration instrument was employed in a preliminary study of the [alpha]-chymotrypsin catalyzed hydrolysis of some acylated amino acid esters. A useable system was developed, and some preliminary results were obtained concerning techniques, data treatment, surface effects and steric effects in enzyme catalyzed reactions.
The kinetics of the [alpha]-chymotrypsin catalyzed hydrolysis of methyl hippurate were re-investigated. In addition, the enzyme-inhibitor dissociation constants of two competitive inhibitors were re-determined. The results are compared with values obtained earlier.
Benzoyl-L-valine methyl ester, a new substrate for this enzyme, was studied in the catalyzed reaction employing the above techniques. Additional refinements in technique and errors in this system are discussed.
A number of potential competitive inhibitors, the N-acetyl amino acid N'-methylamides, were synthesized and tested for inhibitory activity in the [alpha]-chymotrypsin catalyzed hydrolysis of methyl hippurate and benzoyl-L-valine methyl ester. The results indicate that, of the compounds studied, only those containing an aromatic residue have a measurable effect in the present systems.
|Item Type:||Thesis (Dissertation (Ph.D.))|
|Degree Grantor:||California Institute of Technology|
|Division:||Chemistry and Chemical Engineering|
|Thesis Availability:||Public (worldwide access)|
|Defense Date:||1 January 1956|
|Default Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Imported from ETD-db|
|Deposited On:||13 Jul 2004|
|Last Modified:||26 Dec 2012 02:54|
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