title: Biochemistry and physiology of monoamine oxidase (MAO) activity in the ring dove (Streptopelia risoria). I. Characteristics of MAO activity in vitro.
abstract: Monoamine oxidase (MAO) activity was measured in ring dove (Streptopelia risoria) tissues using a fluorometric assay with kynuramine as substrate. Harmaline inhibited MAO activity in a time-dependent manner, and preincubation of enzyme with the drug did not affect its activity. Pargyline produced a slow-onsetting inhibition of activity which was enhanced by preincubation of enzyme and inhibitor. Harmaline displayed reversible non-competitive inhibition of MAO activity. Oxygen is also a substrate for dove MAO, and the reaction apparently involves "ping-pong", double-displacement kinetics. Dove MAO activity is temperature-dependent, with an activation energy of 13.1 kcal/mole.
authors.forename: T R
authors.initials: TR
authors.lastname: Hall
authors.forename: R W
authors.initials: RW
authors.lastname: Lea
authors.forename: D M
authors.initials: DM
authors.lastname: Vowles
authors.forename: S
authors.initials: S
authors.lastname: Harvey
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D010856:Columbidae / Q000378:metabolism*; D005260:Female; D006246:Harmaline / Q000494:pharmacology; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000378:metabolism*; D010293:Pargyline / Q000494:pharmacology; D013816:Thermodynamics; D014018:Tissue Distribution
chemical_list: D010293:Pargyline; D006246:Harmaline; D008995:Monoamine Oxidase