Effect of some monoamine oxidase inhibitors on deamination of biogenic monoamines by rat liver mitochondrial monoamine oxidase

1966 ◽  
Vol 22 (3) ◽  
pp. 157-157 ◽  
Author(s):  
V. Z. Gorkin ◽  
L. I. Gridneva ◽  
L. B. Klyashtorin ◽  
I. V. Veryovkina ◽  
I. Vina
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Monoamine Oxidase Inhibitors ◽  
Biogenic Monoamines ◽  
Mitochondrial Monoamine Oxidase

scholarly journals 5-HYDROXYTRYPTAMINE : A SUBSTRATE FOR RAT LIVER MITOCHONDRIAL MONOAMINE OXIDASE-A AND -B*

1982 ◽  
Vol 32 (5) ◽  
pp. 954-957
Author(s):  
Hiroyasu KINEMUCHI ◽  
Takamori KAWAGUCHI ◽  
Yuichiro ARAI ◽  
Hirohisa TAJIMA ◽  
Lars ORELAND ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Monoamine Oxidase A ◽  
Mitochondrial Monoamine Oxidase

Interactions of Monoamine Oxidase Inhibitors, N-Acetylenic Analogues of Tryptamine, with Rat Liver Microsomal Cytochrome P450

1994 ◽  
Vol 46 (5) ◽  
pp. 360-365
Author(s):  
MASSIMO VALOTI ◽  
MARISA COSTANZO ◽  
GIAN PIETRO SGARAGLI ◽  
VIRGILI PEREZ ◽  
ELDIBERTO FERNANDEZ-ALVAREZ ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Monoamine Oxidase ◽  
Rat Liver ◽  
Monoamine Oxidase Inhibitors ◽  
Microsomal Cytochrome ◽  
Microsomal Cytochrome P450

The effect of tris buffers on rat liver mitochondrial monoamine oxidase

1977 ◽  
Vol 29 (1) ◽  
pp. 411-415 ◽  
Author(s):  
C. J. FOWLER ◽  
B. A. CALLINGHAM ◽  
M. D. HOUSLAY
Keyword(s):  
Monoamine Oxidase ◽  
Rat Liver ◽  
Mitochondrial Monoamine Oxidase

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.

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