"Monoamine oxidase may now be defined as the enzyme which is responsible for the oxidative deamination of such monoamines as adrenaline, butylamine, and tyramine. The enzyme is inhibited by iproniazid (1×10-4 M) but not by cyanide or isoniazid (1×104 M). More recently it has been shown that 5-hydroxytryptamine (serotonin) and 3-4-dihydroxyphenylethylamine (dopamine) are amongst the most rapidly metabolized of the physiologically active substrates of the enzyme." This statement of Davison,1 coupled with the recent availability of specific and irreversible monoamine oxidase inhibitors in increasing numbers,2 attests to the renewed interest in the physiological role of the enzyme and the pharmacological significance of the inhibitors.
These advances in our knowledge of the nature of the enzyme and its inhibitors stimulated the present investigation of their role in the ocular tissues from a functional and therapeutic point of view. It has been shown elsewhere that not only large
KRISHNA N, MANN MJ, LEOPOLD IH. Manometric Determination of Monoamine Oxidase in Ocular Tissues. Arch Ophthalmol. 1961;65(3):338–344. doi:https://doi.org/10.1001/archopht.1961.01840020340005
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