Almond, Harold Russell (1961) I. The consequences of systematic error in enzyme kinetics. II. L-tyrosyl-L-tyrosine derivatives for the detection of transpeptidation in alpha-chymotrypsin-catalyzed hydrolyses. III. The interaction of alpha-methyl-alpha-acylamino acids with alpha-chymotrypsin. IV. The apparent ionization constants of a series of phenylalanine derivatives. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-03272006-084330
NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in .pdf document.
The consequences of systematic error in enzyme kinetics were investigated. Systematic error in substrate blank, enzyme blank, velocity determination, substrate concentration and the Beer-Lambert relationship was considered. The advisability of using weighting procedures in the presence of systematic error was questioned.
L-Tyrosyl-L-tyrosine methyl ester, amide, hydrazide and hydroxamide were prepared in order to detect transpeptidation in alpha-chymotrypsin-catalyzed hydrolyses. The reaction products from the hydrolyses of the corresponding L-tyrosine derivatives were found to contain only negligible amounts of transpeptidation products except for L-tyrosinhydroxamide which gave some L-tyrosyl-L-tyrosine. alpha- and beta-chymotrypsin were qualitatively the same with respect to these reactions.
The N-acetyl methyl esters of alpha-methylphenylalanine, alpha-methyltyrosine and alpha-methyl-beta-(2-naphthyl)-alanine were synthsized and resolved. These esters are good competitive inhibitors of alpha-chymotrypsin. N-acetyl-(-) alpha-methyl-beta-(2-naphthyl)-alanine is a slowly hydrolyzed substrate of this enzyme. The inactivity of these esters toward alpha-chymotrypsin-catalyzed hydrolysis is a consequence of their inability to react further after complexing with the enzyme.
The [...] values of the alpha-ammonium groups of D,L-phenylalanine amide, thioamide, amidoxime, hydrazide, methyl ester and hydroxamide were determined. Comparison of these [...] values with some for corresponding glycine derivatives shows the former to be 0.59 ± .04 pK units lower. The infrared spectra of these phenylalanine derivatives were determined in KBr.
|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 1961|
|Default Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Imported from ETD-db|
|Deposited On:||27 Mar 2006|
|Last Modified:||26 Dec 2012 02:35|
- Final Version
See Usage Policy.
Repository Staff Only: item control page