The oxidation of dopamine and epinine by the two forms of monoamine oxidase from rat liver.
Information on the "in vitro" oxidation of epinine by monoamine oxidase (MAO) compared to dopamine is very poor. The aim of this work was to study the oxidative deamination of epinine and dopamine by rat liver MAO-A and MAO-B. The contributions of MAO-A and B to the metabolism of dopamine (55% and 45%, respectively) and epinine (70% and 30%, respectively) were similar. The results of this study show that epinine is a substrate for both forms of MAO in rat liver, although the contribution of MAO A to the deamination of this secondary amine appears to be slightly more important than that of MAO B.
Strolin Benedetti
M
M
Department of Preclinical Development and Human Pharmacology, Zambon Group, Bresso, Italy.
Sanson
G
G
Bona
L
L
Gallina
M
M
Persiani
S
S
Tipton
K F
KF
D000818:Animals; D003010:Clorgyline / Q000494:pharmacology; D003846:Deoxyepinephrine / Q000378:metabolism*; D004298:Dopamine / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D008995:Monoamine Oxidase / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats; D017207:Rats, Sprague-Dawley; D013379:Substrate Specificity
D007527:Isoenzymes; D008995:Monoamine Oxidase; D003010:Clorgyline; D003846:Deoxyepinephrine; D004298:Dopamine