Inhibition of rat liver monoamine oxidase by alpha-methyl- and N-propargyl-amine derivatives.
The inhibition of rat liver monoamine oxidase by a number of N-propargyl and alpha-methyl amine derivatives has been examined. The results indicate that alpha-methyl-substituted primary and secondary amine derivatives tend to show selectivity as reversible inhibitors towards the A-form of the enzyme. The structural features that result in selectivity in irreversible inhibitors are less easy to define and substitution of an N-propargyl group into a compound that is a selective reversible inhibitor of monoamine oxidase will not necessarily result in retention of that selectivity. Replacement of the acetylenic group in a B-selective irreversible inhibitor by an ethylenic group resulted in a compound that was a reversible inhibitor showing slight selectivity for the A-form of the enzyme.
D000480:Alkynes / Q000494:pharmacology*; D000818:Animals; D066298:In Vitro Techniques; D008744:Methylamines / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008996:Monoamine Oxidase Inhibitors; D011437:Propylamines / Q000494:pharmacology*; D051381:Rats; D013329:Structure-Activity Relationship
D000480:Alkynes; D008744:Methylamines; D008996:Monoamine Oxidase Inhibitors; D011437:Propylamines