Rapp, James R. (1964) Stereospecificity in alpha-chymotrypsin-catalyzed reactions. The structural specificity of alpha-chymotrypsin : some new substrates. A further study of monofunctional aromatic inhibitors of alpha-chymotrypsin. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-10212002-113251
A series of acylated glycine, D and L-alanine methyl esters have been evaluated as substrates for alpha-chymotrypsin. These results are correlated with a theory concerning the stereospecificity of the enzyme.
The effect on the kinetic constants of reducing an aromatic substrate to its hydroaromatic counterpart is studied. Two classes of substrates are distinguished, one in which the ring is in the side chain and the other where the ring is part of the acylamido group.
Several analogues of known substrates are examined and their relationship and importance to the general picture of the specificity of alpha-chymotrypsin are discussed.
A series of simple aromatic inhibitors of alpha-chymotrypsin were examined. Concomitantly, the combined effect of two inhibitors on alpha-chymotrypsin-catalyzed hydrolyses is discussed.
|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 1964|
|Default Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Imported from ETD-db|
|Deposited On:||22 Oct 2002|
|Last Modified:||26 Dec 2012 03:06|
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