A new type of mitochondrial monoamine oxidase distinct from type-A and type-B.

  title={A new type of mitochondrial monoamine oxidase distinct from type-A and type-B.},
  author={Hiroyasu Kinemuchi and M Sudo and Masataka Yoshino and T. Kawaguchi and Y Sunami and Kazuya Kamijo},
  journal={Life sciences},
  volume={32 5},
Enzymic and molecular characteristics of a new form of monoamine oxidase, distinct from form-A and form-B.
By the present definitions ofMAO-A and MAO-B, MAO in carp brain and liver is similar to, but distinct from, both these forms of MAO.
Monoamine oxidase activities in catfish (Parasilurus asotus) tissues.
Catfish brain and liver contain a single form of MAO, relatively similar to mammalian MAO-A, which was determined using 5-hydroxytryptamine, tyramine and beta-phenylethylamine as substrates.
Phospholipid dependency of carp brain and liver mitochondrial monoamine oxidase.
The new generation of monoamine oxidase inhibitors.
  • A. Cesura, A. Pletscher
  • Biology
    Progress in drug research. Fortschritte der Arzneimittelforschung. Progres des recherches pharmaceutiques
  • 1992
In subjects with Parkinson's disease the MAO-B inhibitor L-deprenyl exerts a L-dopa-sparing effect, prolongs L- dopa action and seems to have a favorable influence regarding on-off disabilities.
Comparative Study of Catalytic Properties of Monoamine Oxidases of the Liver of the Squid Todarodes pacificus and of the Liver of the Wistar Rat
It is revealed that the squid liver MAO, unlike the rat liverMAO, is capable of deaminating not only tyramine, serotonin, and benzylamine, but also histamine, and the specificity of action of an irreversible inhibitor, proflavine, is established, which was seen at deamination of various substrates by the squid Liver MAO to the greater degree.
Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.
It is suggested that Triton X-100 had different actions on the enzyme depending on preincubation, depending on the concentration of detergent used, as well as slightly changed enzyme sensitivity towards clorgyline and deprenyl.
Comparative enzymologic study of catalytical properties of liver monoamine oxidases of sturgeon fish
All studied enzymes have been established to have the higher activity toward serotonin and noradrenalin-substrates of the MAO A form as compared with benzylamine, β-phenylethylamin, and N-methylhistamine-substrate of the mammalian MAO B form, the maximal activity being characteristic of the giant sturgeon.
Comparative sensitivity of liver monoamine oxidases of frog and whitefish to some tricyclic compounds
The obtained data of the inhibitory analysis with use of specific substrates are an indirect proof for the existence in liver of the studies frog species of two molecular forms, whereas in the whitefish liver—the single molecular MAO form.
Some characteristics of mitochondrial monoamine oxidase activity in eggs of carp (Cyprinus carpio) and rainbow trout (Salmo gairdneri).
  • A. Nicotra, O. Senatori
  • Biology, Environmental Science
    Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology
  • 1989


5-hydroxytryptamine: a substrate for rat liver mitochondrial monoamine oxidase-A and -B.
The concentration dependence of the oxidation rates of serotonin by the two forms of MAO in rat liver mito chondria is investigated.
Substrate Selectivity of Type A and Type B Monoamine Oxidase in Rat Brain
It is concluded from the present findings that the effect of the substrate concentration must be considered in studies on the characteristics of multiple forms of MAO in various organs and species.
The results indicate that the inhibitory effects of the two inhibitors on the enzyme in circumventricular structures of the brain is time‐ and temperature‐dependent.
Monoamine oxidase A and B: a useful concept?
Deamination of 5‐Hydroxytryptamine by Both Forms of Monoamine Oxidase in the Rat Brain
Abstract: K m and Vmax values of monoamine oxidase (MAO) A and B towards 5‐hydroxytryptamine were determined for rat brain homogenates after the in vitro inhibition of one of the two forms by the
Studies on cytochrome oxidase. III. Improved preparation and some properties.
  • T. Yonetani
  • Chemistry, Biology
    The Journal of biological chemistry
  • 1961