Monoacetylation of 2,4-Diamino-6-Nitrotoluene. Kinetic Studies with α-Chymotrypsin. Effect of Dilantin Upon Ether Narcosis in the Cat
Author: Foster, Robert Joseph
Year: 1952
Degree: Dissertation (Ph.D.)
Advisor: Niemann, Carl G.
Committee Member: Unknown, Unknown
Option: Chemistry; Biology
DOI: 10.7907/K13Z-9D57
Abstract
The structure of the monoacetyl derivative of 2,4-diamino-6-nitrotoluene formed by reaction with an equimolar quantity of acetic anhydride in dry acetone at room temperature has been shown to be 2-amino-4-acetamido-6-nitrotoluene.
The kinetic constants for the enantiomorphic pair of acetyl-phecylalaninamides and α-chymotrypsin at 25°and pH 7.9 in aqueous solution have been determined. The relationships of these constants with others determined for similar enantiomorphic pairs is discussed. Equations for the competitive hydrolysis of two substrates at the same catalytically active site of an enzyme have been derived and have been tested experimentally.
The kinetic constants for L-tyrosine-hydroxamide and α-chymotrypsin have been determined at pH 6.9 and 25°. With this hydroxamide as substrate, the enzyme-inhibitor complex dissociation constants have been determined for a series of inhibitors at pH 6.9 and 25°. The differences between these constants and those at pH 7.9 is discussed and the charge state of the catalytically active site is inferred.
The effect of the anti-convulsant dilantin upon ether narcosis in the cat has been determined and is discussed in its relation to present theories of nervous propagation and narcosis.
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