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Substrate specificity of mitochondrial monoaminoxidase from rat liver and binding of enzyme and substrate into enzyme-substrate complex



Substrate specificity of mitochondrial monoaminoxidase from rat liver and binding of enzyme and substrate into enzyme-substrate complex



Biokhimiya 32(4): 843-853



The effect of heating, treatment with urine, and other factors upon the ability of rat liver mitochondrial monoaminoxidase (MAO) (E. C. 1.4.3.4) to catalyze deamination of thyramine, serotonin, benzylamine, and phenylethylamine derivatives was studied. The present data support the suggestion that selective inhibition of the oxidative deamination of amines with preparations of mitochondrial MAO from rat liver treated with various denaturing factors, may be the result of changes in the conformation of protein and differences in the chemical structure of substrates.

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