scholarly journals The influence of respiratory state on monoamine oxidase activity in rat liver mitochondria

1978 ◽  
Vol 176 (3) ◽  
pp. 1011-1014 ◽  
Author(s):  
G S Smith ◽  
R A Reid
Keyword(s):  
Monoamine Oxidase ◽  
Outer Membrane ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Monoamine Oxidase Activity ◽  
Oxidative Deamination ◽  
Thermodynamic State ◽  
Respiratory State

Changes in the respiratory state of rat liver mitochondria caused significant changes (up to 10-fold) in the rates of oxidative deamination of tyramine, indicating interactions between the inner coupling membrane and the monoamine oxidase sites in the outer membrane, and suggesting the possibility that monoamine oxidase is regulated by the thermodynamic state of the mitochondria.

Polyacrylaniide Gel Electrophoresis of Rat Liver Mitochondrial Monoamine Oxidases

1973 ◽  
Vol 51 (7) ◽  
pp. 1089-1095 ◽  
Author(s):  
J. M. Diaz Borges ◽  
A. D'Iorio
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Oxidase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Liver Mitochondria ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Monoamine Oxidase Activity ◽  
Tetrazolium Staining

Solubilized rat liver mitochondria were subjected to polyacrylamide gel electrophoresis. The monoamine oxidase activity was localized directly on the gel with radioactive substrates (serotonin, benzylamine, and tyramine). Serotonin and tyramine monoamine oxidase activity separated in several bands which migrated to the anode and cathode whereas benzylamine activity was localized in one band. This band was demonstrated only when the electrophoresis was run from cathode to anode. Each one of tyramine and serotonin activities could be found devoid of the other two activities. Benzylamine activity could be separated from the serotonin activity though not from the tyramine activity. The detection of monoamine oxidase with the tetrazolium staining provided a localization of the enzyme activity which was different from that observed using radioactive substrates. These results, in accordance with those previously obtained by us with sucrose gradient electrophoresis of the same preparation, support the existence of different enzymes for the oxidative deamination of benzylamine and serotonin. On the other hand our results did not eliminate the possibility of overlapping substrate specificity of tyramine activity with those of serotonin and benzylamine activities.

Multiple monoamine oxidases in rat liver mitochondria

1970 ◽  
Vol 48 (6) ◽  
pp. 659-663 ◽  
Author(s):  
L. Sierens ◽  
A. D'Iorio
Keyword(s):  
Rat Liver ◽  
Indirect Evidence ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Electrophoretic Separation ◽  
Oxidative Deamination ◽  
Monoamine Oxidases ◽  
Kinetics Of

Indirect evidence from the kinetics of oxidative deamination is presented for the existence of two different monoamine oxidases in rat liver mitochondria. The enzymes can be differentiated on the basis of their affinities for benzylamine and serotonin. Electrophoretic separation yielded two fractions, each with the characteristics predicted from the kinetic experiments.

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