Über die Reduktion der Katalase
- 1 January 1940
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 263 (3-5) , 181-186
- https://doi.org/10.1515/bchm2.1940.263.3-5.181
Abstract
It was not possible to reduce catalase with Na2S2O4, by H2 activated by catalysts, or by yeast. Catalase was prepared from horse liver under anaerobic conditions, but the product obtained was not very pure. The normal or oxidized form of catalase had an absorption band at 629 m[mu], while the reduced form did not show this band. When catalase was treated with H2S, the resulting compound reduced with Na2S2O4, and the H2S removed, catalase was regenerated by oxidation with air. Neither cysteine nor glutathione could take the place of H2S in this reaction, but washed liver slices could be used. These reactions might lead to a better understanding of the function of catalase in the living cell.This publication has 3 references indexed in Scilit:
- On the haematin compound of peroxidaseProceedings of the Royal Society of London. B. Biological Sciences, 1937
- SPECTROSCOPY OF CATALASEThe Journal of general physiology, 1937
- On the combinations of methæmoglobin with H 2 SProceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character, 1933