THE ACTION OF p-AMINOPHENOL ON THE XANTHINE OXIDASE OF LIVER
نویسنده
چکیده
The quinimine form of p-aminophenol inhibits the oxygen uptake of tissue suspensions and in very small concentrations inhibits specifically the oxidation of hypoxanthine and xanthine to uric acid by the xanthine oxidase of liver (1). Closely related compounds such as o-aminophenol, p-phenylenediamine, and quinone, although they inhibit to different degrees the oxygen uptake of tissues, have no effect on the xanthine oxidase. Because none of the other common dehydrogenases is affected by the quinimine and because the xanthine oxidase is inhibited by it in concentrations as low as 0.00001 M, it was of interest to study the mechanism of the inhibition more closely.
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