US EPA

7902408 

Journal Article 

[Deamination reaction of biogenic amines and other nitrogen compounds during the long-term influence of ethylenediamine in an experiment on rats] 

Fukalova, LA; Dubinina, ON 

1992 

1 

Voprosy Meditsinskoĭ Khimii
ISSN: 0042-8809 

38 

2 

23-25 

Russian 

1413623 

Activity and substrate specificity of monoamine oxidase (MAO) were studied in tissues of rats inhaling low concentrations of ethylene diamine for a long time. While the activity of MAO-A (serotonin as a substrate) was decreased in brain, functions of the enzyme were altered: the enzyme acquired the ability to deaminate glucosamine, which is not a substrate of MAO under normal conditions. Ethylene diamine-dependent modification of MAO was responsible for alterations of the enzyme catalytic properties involved in oxidation of substances with specific biochemical functions. A new drug diethon as well as ionol, pyrazidole and ascorbic acid were used in attempts to normalize the MAO properties; ionol proved to be the most effective compound. Detection of alterations in the MAO catalytic properties, developed after influence of the chemical factor at very low concentrations but without symptoms of toxicosis, may be used as a sensitive test for evaluation of early steps of ethylene diamine-produced intoxication. Ionol may be used for pathogenetic prophylaxis of ethylene diamine caused intoxication.