Author:
Walterová Daniela,Kovář Jan,Preininger Vladimír,Šimánek Vilím
Abstract
The interaction between horse liver alcohol dehydrogenase (ADH) and aporphine alkaloids has been studied by kinetic and fluorescence methods. The aporphine alkaloids inhibit ADH. The inhibitory effect depends on the position and type of the substituents in the aporphine nucleus. Aporheine shows the strongest binding to the enzyme, and that irrespective of the configuration of the molecule. The dissociation constant of the complex enzyme-aporpheine is 20-25μmol l-1. The results indicate that the aporphine alkaloids bind to the active center of alcohol dehydrogenase with stechiometry 1 : 1.
Publisher
Institute of Organic Chemistry & Biochemistry
Cited by
6 articles.
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