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Abstract
1. The enzymic deacetylation of 4-acetamidobenzoate by the liver and kidney of the rat, rabbit, mouse and guinea-pig has been examined. The most active tissue was rat kidney which was examined in detail.
2. In the rat kidney the enzyme activity was found in the cell sap. This activity was considerably increased by Mn2+ ions but completely inhibited by Hg2+ ions.
3. The Mn2+ ion dependent activity, but not the Mn2+ ion independent activity, was inhibited by p-chloromercuribenzoate, thioglycollate, CoA, acetyl-CoA, storage at 5°, Sephadex filtration and dimethylsulphoxide. It is suggested that Mn2+ ions activate the enzyme allosterically.
4. 4-Acetamidobenzoate deacetylase activity was not found in rat brain, blood or skeletal muscle and only low activity was found in liver, heart muscle, spleen and lung.
5. The rat kidney cell sap enzyme had only slight activity towards acetanilide and none towards N4-acetylsulphanilamide. Acetanilide was deacetylated mainly by the microsomal fraction of rat kidney homogenates.