Aldehyde mutase
- 1 August 1937
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 31 (8) , 1347-1365
- https://doi.org/10.1042/bj0311347
Abstract
Aldehyde oxidase (Schardinger enzyme) did not dismute aldehydes, did not depend on coen-zymes for its activity, was inactivated by cyanide but not by iodoacetate and acted on both aliphatic and aromatic aldehydes. Aldehyde mutase dismuted but did not oxidize aldehydes, depended on cozymase for its activity, was inactivated by iodoacetate but not by cyanide and acted on aliphatic but not on aromatic aldehydes. Aldehyde mutase was evidently a distinct enzyme or enzyme system. Neither aldehyde oxidase nor alcohol dehydro-genase was a component of the mutase system. Purified cozymase (ACo 600,000) acted very efficiently as comutase. Coenzyme II (Warburg coenzyme), adenylpyrophosphate, trigonellin and glutathione were inactive.This publication has 4 references indexed in Scilit:
- The measurement of tissue glycolysis in serumBiochemical Journal, 1937
- The aldehyde oxidase of the potatoBiochemical Journal, 1928
- On the Further Purification of the Xanthine OxidaseBiochemical Journal, 1926
- Studies on Xanthine OxidaseBiochemical Journal, 1924