Preparation of purified 3-hydroxyanthranilic acid oxidase from rat and ox liver

Publisher Website
Google Scholar
Abstract
3-Hydroxyanthranilic acid oxidase has been purified from rat and ox liver. The most active preparations of the enzyme oxidize 2500 um moles of 3-hydroxyanthranilic acid/min./mg of protein. The dependence of the reaction rate on the concentration of both substrates (3-hydroxyanthranilic acid and oxygen) was measured. Km for 3-hydroxyanthranilic acid is low (7 ([mu]M under the conditions of the activity test). At the oxygen pressure of the air the reaction rate is still far from maximal. The purified enzyme solutions present an absorption maximum at 400 m[mu] and a peculiar fluorescence. There is not yet sufficient evidence to ascertain whether these bands are due to the enzyme itself or to impurities.