Effect of alcohols on mitochondrial monoamine oxidase activity

1975 ◽  
Vol 79 (1) ◽  
pp. 30-32 ◽  
Author(s):  
I. S. Severina
Keyword(s):  
Monoamine Oxidase ◽  
Oxidase Activity ◽  
Monoamine Oxidase Activity ◽  
Mitochondrial Monoamine Oxidase

On hepatic mitochondrial monoamine oxidase activity in lipid deficiency

1979 ◽  
Vol 57 (6) ◽  
pp. 588-594 ◽  
Author(s):  
C. Kandaswami ◽  
A. D'Iorio
Keyword(s):  
Fatty Acids ◽  
Monoamine Oxidase ◽  
Oxidase Activity ◽  
Marked Decrease ◽  
Specific Activity ◽  
Essential Fatty Acids ◽  
Mitochondrial Outer Membrane ◽  
Monoamine Oxidase Activity ◽  
Membrane Enzyme ◽  
Mitochondrial Monoamine Oxidase

A marked decrease in liver mitochondrial monoamine oxidase activity was noticed in rats fed a fat-free diet as compared with that of their controls. In lipid-deprived rats, the specific activity of this enzyme was very low towards different substrates studied. The activity of kynurenine 3-monooxygenase, which like monoamine oxidase is localized on the mitochondrial outer membrane, was similarly depressed under conditions of lipid deprivation. On the other hand no major changes were observed in the activity of the inner membrane enzyme, kynurenine aminotransferase. Mitochondria from fat-free diet-fed rats were deficient in essential fatty acids whereas no appreciable variations were found in the relative proportions of phospholipids in comparison with those of control mitochondria. Mitochondrial monoamine oxidase activity of the deficient rats retained its sensitivities to inhibitor drugs like clorgyline and deprenyl. No changes were noticeable in the substrate specificity of monoamine oxidase in these rats. When we switched the fat-free diet-fed rats to a diet supplemented with a source of essential fatty acids, there was an elevation in the activities of both monoamine oxidase and kynurenine 3-monooxygenase, their levels approaching those of the control rats.

Possible isoenzymes of monoamine oxidase in rat tissues

1968 ◽  
Vol 46 (4) ◽  
pp. 295-297 ◽  
Author(s):  
H. C. Kim ◽  
A. D'Iorio
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Liver Homogenate ◽  
Rat Tissues ◽  
Consistent Difference ◽  
Monoamine Oxidase Activity ◽  
Mitochondrial Monoamine Oxidase

The solubilized monoamine oxidase activity of rat liver, kidney, and brain can be separated into several bands by cellulose polyacetate membrane electrophoresis. Four such bands of activity are found in the whole liver homogenate while mitochondrial and microsomal fractions appear to have two. The activity of these bands has been assayed using three different substrates, isoamylamine, tyramine, and benzylamine. The solubilized mitochondrial monoamine oxidase activity of kidney and brain when submitted to electrophoresis is found to separate in two fractions. There is some small but consistent difference of distribution of activity when using different substrates.

In vitro and in vivo effect of chloropromazine, imipramine and lithium chloride on monoamine oxidase activity in rat brain mitochondria

1987 ◽  
Vol 7 (9) ◽  
pp. 701-704 ◽  
Author(s):  
Maitreyi Nag ◽  
Namita Nandi
Keyword(s):  
Monoamine Oxidase ◽  
Rat Brain ◽  
Dose Level ◽  
Lithium Chloride ◽  
Oxidase Activity ◽  
Brain Mitochondria ◽  
Monoamine Oxidase Activity ◽  
Mitochondrial Monoamine Oxidase

Chloropromazine (CPZ) and imipramine at a concentration of 1×10−3 M inhibit rat brain mitochondrial monoamine oxidase activity in vitro by 70 and 55% respectively, while lithium, even at a concentration of 0.05 M, inhibits the activity of this enzyme very negligibly (4%). In vivo, these drugs at a dose level of 56 mg CPZ, 76 mg Jimipramine and 76 mg lithium chloride/Kg body wt., did not cause any observable variation from normal in brain mitochondrial monoamine oxidase activity.

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