ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINE VI. INHIBITION OF GLYOXALASE ACTIVITY OF HUMAN AND RABBIT ERYTHROCYTES
- 1 June 1953
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Medical Sciences
- Vol. 31 (3) , 195-201
- https://doi.org/10.1139/cjms53-021
Abstract
Phenothiazone has been found to be a strong inhibitor of glyoxalase activity of human and rabbit erythrocytes. Concentrations for 50% inhibition were 10−6 M for intact cells and 10−4 M for haemolysates with added glutathione. Glyoxalase activity was also markedly inhibited by phenothiazine, methylene blue, and p-chloromercuribenzoate; slightly inhibited by alloxan and phenylhydrazine; and not affected by dialuric acid. Enzyme inhibition did not parallel methaemoglobin formation. The possible relationship of these findings to the haemolytic action of phenothiazine is discussed.Keywords
This publication has 7 references indexed in Scilit:
- ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINECanadian Journal of Medical Sciences, 1952
- ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINECanadian Journal of Medical Sciences, 1952
- Glyoxalase: the role of the componentsBiochemical Journal, 1952
- The binding of thiazines by proteins and nucleic acidArchives of Biochemistry and Biophysics, 1952
- THE MECHANISM OF ACTION OF GLYOXALASEJournal of Biological Chemistry, 1951
- INHIBITION OF SUCCINIC DEHYDROGENASE BY METHYLGLYOXALJournal of Biological Chemistry, 1950
- The glyoxalase activity of the red blood cell. The function of glutathione.1933