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The effect of lipophilic compounds upon the activity of rat liver mitochondrial monoamine oxidase-A and -B
Authors:Christopher J Fowler  Brian A Callingham  Timothy J Mantle  Keith F Tipton
Institution:Department of Pharmacology, University of Cambridge, Hills Road, Cambridge, CB2 2QD, U.K.;Biochemistry Department, Trinity College, Dublin 2, Ireland
Abstract:The effect of various lipophilic compounds on the activity of monoamine oxidase (MAO) was determined. The local anaesthetics procaine, procainamide, tetracaine and lignocaine were all MAO-A selective inhibitors, whereas benzyl alcohol, butan-l-ol, hexan-l-ol and octan-l-ol inhibited MAO-B selectively. Procaine was found to be a competitive inhibitor of the deamination of 5-hydroxy-tryptamine (5-HT), tyramine, β-phenethylamine and benzylamine. Benzyl alcohol was competitive towards β-phenethylamine and benzylamine, but a mixed-type inhibitor towards 5-HT and tyramine. The same patterns of inhibition for both drugs were found when the activity was assayed under atmospheres of either oxygen or air. The inhibition produced by both compounds was fully reversible. Triton X-100 appeared to inhibit the activity of MAO-A selectively when preincubated with the enzyme for 30 min at 30°. This selectivity was lost when the preincubation temperature was raised to 37°. The inhibition of MAO activity by Triton X-100 after preincubation at 37° was found to be irreversible. Sodium deoxycholate and SDS were also found to inhibit the activity of MAO after preincubation with the enzyme at 37°. The significance of these results is discussed.
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