Solvent isotope effects on formation of protease complexes with inhibitory aldehydes
R Bone, R Wolfenden
Index: Bone, Roger; Wolfenden, Richard Journal of the American Chemical Society, 1985 , vol. 107, # 16 p. 4772 - 4777
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Citation Number: 27
Abstract
Abstract: In both CC14 and water, equilibria of addition of thiols to acetaldehyde are strongly favored by the presence of deuterium at exchangeable positions, whereas equilibria of addition of hydroxylic compounds are hardly affected. To test the possibility of using solvent isotope effects for diagnosing the structure of enzyme-inhibitor complexes, we examined the influence of D 2 0 on the interaction of proteases with inhibitory aldehydes. Equilibrium ...
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