The effect of lipophilic compounds upon the activity of rat liver mitochondrial monoamine oxidase-A and -B.

@article{Fowler1980TheEO,
  title={The effect of lipophilic compounds upon the activity of rat liver mitochondrial monoamine oxidase-A and -B.},
  author={Christopher John Fowler and Brian A. Callingham and Timothy J. Mantle and Keith F. Tipton},
  journal={Biochemical pharmacology},
  year={1980},
  volume={29 8},
  pages={
          1177-83
        }
}
Effect of Lignocaine on Tyramine and Serotonin Oxidation in Brain
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Nothing is known about lignocaine’s effect on the oxidation of monoamines in relation to the changes in the kinetic properties of brain MAO.
Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.
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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.
Deamination of aliphatic amines of different chain lengths by rat liver monoamine oxidase A and B
  • P. Yu
  • Chemistry, Biology
    The Journal of pharmacy and pharmacology
  • 1989
TLDR
All these aliphatic amines are found to be typical type B substrates according to the sensitivities of the enzyme towards the selective MAO‐B inhibitor selegiline and theMAO‐A inhibitor, clorgyline.
Can our knowledge of monoamine oxidase (MAO) help in the design of better MAO inhibitors?
  • P. Dostert
  • Biology, Chemistry
    Journal of neural transmission. Supplementum
  • 1994
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It is suggested that MAO inhibition might be advantageously combined with other pharmacological properties for the treatment of pathological conditions, such as stroke and epilepsy, to the occurrence of which MAO activity might contribute.
...
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The effect of tris buffers upon the monoamine oxidase (MAO) activity in rat liver mitochondria has been investigated and it is suggested that these effects are produced by conformational changes in the structure of the MAO.
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TLDR
Treatment of a preparation of rat liver monoamine oxidase with the chaotropic agent sodium perchiorate seemed to render the enzyme homogeneous by a number of criteria without any significant loss of activity, giving further support to the view that the multiple forms are caused by the association of lipid membrane material with a single enzyme.
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