1. The purification and properties of arginine decarboxy-oxidase present in Streptomyces griseus (Waksman) are described. The enzyme is highly specific. 2. 2. The stoichiometry of the enzymic reaction has been investigated. Thus, the ratio of arginine oxidized to oxygen absorbed to carbon dioxide evolved is 1:1:1. This ratio is not modified by the presence of catalase. The reaction does not occur anaerobically in the presence of ferricyanide. 3. 3. The enzyme is inactivated by oxygen. In the presence of arginine as substrate this inactivation is reduced. Sulfhydryl reagents similarly show less inhibitory activities in the presence of the substrate. 4. 4. Besides Str. griseus, several other species of Acetomyces have been shown to have arginine decarboxy-oxidase activity.
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Nguyen-Van-Thoai et al. (1962) studied this question.
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