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
        }
}
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64 Citations
Background Citations
3
Methods Citations
1

64 Citations

Concentration dependence of the oxidation of tyramine by the two forms of rat liver mitochondrial monoamine oxidase.
Studies of monoamine oxidases. Effect of triton X-100 and bile salts on monoamine oxidase in brain mitochondria.
HPLC-UV assays for evaluation of inhibitors of mono and diamine oxidases using novel phenyltetrazolylalkanamine substrates.
Effect of Lignocaine on Tyramine and Serotonin Oxidation in Brain
TLDR
Nothing is known about lignocaine’s effect on the oxidation of monoamines in relation to the changes in the kinetic properties of brain MAO.
In vivo relationship between monoamine oxidase type B and alcohol dehydrogenase: effects of ethanol and phenylethylamine.
Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.
TLDR
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.
Alterations in monoamine oxidase activity after single and repeated exposure of rats to chlorphentermine.
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.
Inhibition of monoamine oxidase types A and B by 2-aryl-4H-1,3,4-oxadiazin-5(6H)-one derivatives
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
TLDR
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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References

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Inhibition of monoamine oxidase by amphetamine and related compounds.
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TLDR
The results suggest that addition of ethanol does not affect the dissociation constant of the enzyme-substrate complex, but accelerates reaction steps occurring after the enzymes- Substrate complex has been formed.
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EVIDENCE FOR A SINGLE CATALYTIC BINDING SITE ON HUMAN BRAIN TYPE B MONOAMINE OXIDASE
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TLDR
Results suggest that PEA and BzNH2 share a common catalytic binding site on the B form of MAO and, in addition, bind to an inhibitory sites on the reduced form of the oxidase, and indicate that amitriptyline also binds to both the oxidized and reduced forms of this human brain oxidase.
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TLDR
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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