Collect. Czech. Chem. Commun. 1982, 47, 296-303
https://doi.org/10.1135/cccc19820296

Interaction between horse liver alcohol dehydrogenase and aporphine alkaloids

Daniela Walterováa, Jan Kovářb, Vladimír Preiningera and Vilím Šimáneka

a Institute of Medical Chemistry, Medical Faculty, Palacký University, 775 15 Olomouc
b Institute of Biochemistry, Faculty of Natural Sciences, University J. E. Purkyně, 611 37 Brno

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.