Spectrophotometric assay for measuring polyol dehydrogenase activity v1 (protocols.io.natdaen)

protocols.io ◽  
2018 ◽  
Author(s):  
Alexandre Lobo ◽  
V tor
Keyword(s):  
Dehydrogenase Activity ◽  
Spectrophotometric Assay ◽  
Polyol Dehydrogenase

scholarly journals Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity

2020 ◽  
Vol 29 (12) ◽  
pp. 2387-2397
Author(s):  
Diane Chauliac ◽  
Qingzhao Wang ◽  
Franz J. St. John ◽  
Grace Jones ◽  
Jason C. Hurlbert ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Structure Analysis ◽  
Kinetic Characterization ◽  
Lactate Dehydrogenase Activity ◽  
Polyol Dehydrogenase

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.

THE INFLUENCE OF HAEMOGLOBIN-S AND G6PD DEFICIENCY ON THE ACTIVITY OF THE 17β-HYDROXYSTEROID DEHYDROGENASE OF INTACT HUMAN ERYTHROCYTES

1974 ◽  
Vol 75 (4) ◽  
pp. 793-800
Author(s):  
A. O. Sogbesan ◽  
O. A. Dada ◽  
B. Kwaku Adadevoh
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Sex Steroids ◽  
G6pd Deficiency ◽  
Incubation Medium ◽  
Hydroxysteroid Dehydrogenase ◽  
G6pd Activity ◽  
Reverse Transformation ◽  
Oxidative Transformation ◽  
Haemoglobin S

ABSTRACT The 17β-hydroxysteroid dehydrogenase activity in intact erythrocytes of Nigerian patients, in particular with regard to haemoglobin genotypes and G6PD* activity was studied. The G6PD activity of the erythrocyte did not affect the oxidative transformation of testosterone to androstenedione and of oestradiol to oestrone. The reduction (reverse transformation) was inhibited in G6PD-deficient erythrocytes but this inhibition was offset by the addition of 0.025 m glucose to the incubation medium. The per cent oxidation transformation of testosterone was higher in Hb-AA than in Hb-SS erythrocytes. It is suggested that the differences may be a result of either lower enzyme activity in the Hb-SS erythrocytes or of differences in the uptake and possibly binding of sex steroids by intact Hb-SS and Hb-AA erythrocytes.

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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