Liver xanthine oxidase
- 1 December 1936
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 30 (12) , 2166-2176
- https://doi.org/10.1042/bj0302166
Abstract
The self-respiration of minced ox liver was found to be due mainly to purine-base oxidation and was controlled by the rate of formation of the latter by nucleosidase action. Methods are given for the preparation of xanthine oxidase from liver. The kinetics of aldehyde and xanthine oxidation were studied manometrically, making a correction for the oxidation of aldehydes in the presence of alkali. The Km for acetaldehyde was 0.005 M. The enzyme was destroyed by aldehydes. It contains catalase and the cyanide inhibition of xanthine oxidation is due to destruction of this catalase. Oxidation of aldehydes by both minced liver and enzyme preparations was inhibited by xanthine and other purine derivatives.This publication has 10 references indexed in Scilit:
- The identity of xanthine oxidase and the Schardinger enzymeBiochemical Journal, 1935
- The formation of carbohydrate from fat in the liver of the ratBiochemical Journal, 1935
- Studies on xanthine oxidaseBiochemical Journal, 1934
- The oxidation of hexosediphosphoric acid by an enzyme from animal tissuesBiochemical Journal, 1931
- Glucose dehydrogenase: a new oxidising enzyme from animal tissuesBiochemical Journal, 1931
- The effect of narcotics on some dehydrogenasesBiochemical Journal, 1931
- The use of the Barcroft apparatus for the measurement of tissue respirationBiochemical Journal, 1930
- Uricase and its actionBiochemical Journal, 1930
- Studies on Xanthine OxidaseBiochemical Journal, 1925
- Studies on Xanthine OxidaseBiochemical Journal, 1924