ERRATUM: ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINE: VII. INHIBITION OF GLUCOSE-6 PHOSPHATE DEHYDROGENASE ACTIVITY OF RABBIT ERYTHROCYTES

1965 ◽  
Vol 43 (5) ◽  
pp. 623-623
Author(s):  
H. B. Collier ◽  
M. W. Gray
1965 ◽  
Vol 43 (1) ◽  
pp. 105-110 ◽  
Author(s):  
H. B. Collier ◽  
M. W. Gray

The effects of various phenothiazine derivatives were tested, by a NADP+-coupled spectrophotometric assay, on the glucose-6-phosphate dehydrogenase activity of hemolysates of rabbit erythrocytes. Phenothiazine, phenothiazine sulfoxide, thionol, promazine, chlorpromazine, and methylene blue were relatively weak inhibitors. Powerful inhibitors (concentration, for 50% inhibition, I50, in parentheses) were phenothiazone (90 μM) and New Methylene Blue N (75 μM). These two compounds caused a slow direct oxidation of NADPH; however, they appeared to exert an action on the enzyme as well. The enzyme was not inhibited by 2,6-dichlorophenol–indophenol, which is employed in a dye-reduction assay.The enzyme system was readily inactivated by ethanol (I5o = 1.4 M). Prior addition of NADP+ afforded some protection.


1968 ◽  
Vol 59 (3) ◽  
pp. 508-518
Author(s):  
J. D. Elema ◽  
M. J. Hardonk ◽  
Joh, Koudstaal ◽  
A. Arends

ABSTRACT Acute changes in glucose-6-phosphate dehydrogenase and isocitrate dehydrogenase activity in the zona glomerulosa of the rat adrenal cortex were induced by peritoneal dialysis with 5 % glucose. Although less clear, the activity of 3β-ol-hydroxysteroid dehydrogenase also seemed to increase as well. No changes were seen in the activity of succinate dehydrogenase. Dialysis with 0.9 % NaCl had no effect on any of the enzymes investigated. The possible significance of these observations is discussed.


2014 ◽  
Vol 15 (1) ◽  
Author(s):  
Shivang S Shah ◽  
Alex Macharia ◽  
Johnstone Makale ◽  
Sophie Uyoga ◽  
Katja Kivinen ◽  
...  

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