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

1965 ◽  
Vol 43 (1) ◽  
pp. 105-110 ◽  
Author(s):  
H. B. Collier ◽  
M. W. Gray
Keyword(s):  
Methylene Blue ◽  
Dehydrogenase Activity ◽  
Enzyme Inhibition ◽  
Enzyme System ◽  
Spectrophotometric Assay ◽  
Direct Oxidation ◽  
Phenothiazine Derivatives ◽  
Dye Reduction ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Derivatives Of

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.

ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINE: II. INHIBITION OF CHOLINESTERASE

1942 ◽  
Vol 20b (9) ◽  
pp. 189-193 ◽  
Author(s):  
H. Bruce Collier ◽  
Della E. Allen
Keyword(s):  
Methylene Blue ◽  
Alkaline Phosphatase ◽  
Enzyme Inhibition ◽  
Cholinesterase Activity ◽  
Horse Serum ◽  
Phenothiazine Derivatives ◽  
Serum Lipase ◽  
Derivatives Of

The cholinesterase activity of horse serum is strongly inhibited by phenothiazone and by some phenothiazine alkyl-sulphonium salts. The magnitude of this inhibition is about equal to that produced by methylene blue and by acriflavine. Alkaline phosphatase and serum lipase are not affected.The possible relation of this property of phenothiazine derivatives to certain nervous symptoms observed in treated pigs, and to insecticidal and anthelmintic action, is discussed.

ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINE VI. INHIBITION OF GLYOXALASE ACTIVITY OF HUMAN AND RABBIT ERYTHROCYTES

1953 ◽  
Vol 31 (3) ◽  
pp. 195-201
Author(s):  
H. B. Collier ◽  
Sheila C. McRae
Keyword(s):  
Methylene Blue ◽  
Enzyme Inhibition ◽  
Strong Inhibitor ◽  
Intact Cells ◽  
Relationship Of ◽  
Derivatives Of

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.

scholarly journals Acute Hemolytic Anemia in the Newborn Infant due to Naphthalene Poisoning: Report of Two Cases, with Investigations into the Mechanism of the Disease

Blood ◽  
1958 ◽  
Vol 13 (12) ◽  
pp. 1113-1125 ◽  
Author(s):  
JEAN P. DAWSON ◽  
WILLIAM W. THAYER ◽  
JANE F. DESFORGES ◽  
Alice C. Manchester ◽  
Reda Lendraitis
Keyword(s):  
Methylene Blue ◽  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Hemolytic Anemia ◽  
Newborn Infant ◽  
Reductase Activity ◽  
Newborn Period ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract 1. Two cases of naphthalene hemolytic anemia in the newborn period are reported. 2. Both exhibited glutathione instability upon incubation with acetyl phenylhydrazine and naphthol months to years later. Several members of their families exhibited a similar defect with evidence that it is inherited as a simple dominant. 3. In those individuals with glutathione instability there was deficient TPNH2 generation by their hemolysates in the presence of glucose-6-phosphate and TPN, indicating a deficiency in glucose-6-phosphate dehydrogenase activity. Glutathione reductase activity was normal or decreased. 4. TPNH2-linked reduction of methemoglobin by erythrocyte suspensions in the presence of glucose and methylene blue was also decreased in those subjects tested, a finding consistent with the deficiency in glucose-6-phosphate dehydrogenase.

ACUTE ENZYME HISTOCHEMICAL CHANGES IN THE ZONA GLOMERULOSA OF THE RAT ADRENAL CORTEX

1968 ◽  
Vol 59 (3) ◽  
pp. 508-518
Author(s):  
J. D. Elema ◽  
M. J. Hardonk ◽  
Joh, Koudstaal ◽  
A. Arends
Keyword(s):  
Peritoneal Dialysis ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adrenal Cortex ◽  
Isocitrate Dehydrogenase ◽  
Hydroxysteroid Dehydrogenase ◽  
Zona Glomerulosa ◽  
Acute Changes ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Histochemical Changes

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.

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