Glucose-6-Phosphate Dehydrogenase Activity of Rat Liver

Nature ◽  
1952 ◽  
Vol 170 (4316) ◽  
pp. 119-120 ◽  
Author(s):  
G. E. GLOCK ◽  
P. McLEAN
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Glucose 6 Phosphate Dehydrogenase

scholarly journals Characterization of the glucose 6-phosphate dehydrogenase activity in rat liver mitochondria

1976 ◽  
Vol 159 (3) ◽  
pp. 683-687 ◽  
Author(s):  
M Grunwald ◽  
H Z Hill
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Kinetic Behaviour ◽  
Two Peaks ◽  
Glucose 6 Phosphate Dehydrogenase

Glucose 6-phosphate dehydrogenase activity in rat liver mitochondria can be released by detergent. The released activity is separated by chromatography into two peaks. One peak has the kinetic behaviour and mobility similar to the soluble sex-linked enzyme, whereas the other peak is similar to the microsomal hexose 6-phosphate dehydrogenase. There is no evidence for the existence of a new glucose 6-phosphate dehydrogenase activity in rat liver mitochondria.

scholarly journals A critical appraisal of the effect of oxidized glutathione on hepatic glucose 6-phosphate dehydrogenase activity

1983 ◽  
Vol 214 (3) ◽  
pp. 959-965 ◽  
Author(s):  
H R Levy ◽  
M Christoff
Keyword(s):  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Critical Appraisal ◽  
Oxidized Glutathione ◽  
Assay Procedure ◽  
Low Concentrations ◽  
Hepatic Glucose ◽  
Spurious Effect ◽  
Glucose 6 Phosphate Dehydrogenase

Experiments were undertaken to elucidate the mechanism of the reversal of NADPH inhibition of rat liver glucose 6-phosphate dehydrogenase by oxidized gluthathione alone and in combination with a putative cofactor described by Eggleston & Krebs [(1974) Biochem. J. 138, 425-435]. Evidence is presented that this reversal is largely an artifact, caused by the incorrect application of a control assay procedure and a spurious effect of Zn2+ (added in order to inhibit glutathione reductase) in crude enzyme solutions. When the proper assay procedure is used and glutathione reductase is inhibited with low concentrations of Hg2+, glutathione addition has no effect on NADPH inhibition of glucose 6-phosphate dehydrogenase. No evidence was found for the existence of a cofactor that mediates an effect of glutathione on glucose 6-phosphate dehydrogenase.

scholarly journals Lowering Effect of Firefly Squid Powder on Triacylglycerol Content and Glucose-6-Phosphate Dehydrogenase Activity in Rat Liver

2014 ◽  
Vol 63 (12) ◽  
pp. 1293-1301 ◽  
Author(s):  
Hiroyuki Takeuchi ◽  
Ritsuko Morita ◽  
Yoko Shirai ◽  
Yoshihisa Nakagawa ◽  
Teruya Terashima ◽  
...  
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Lowering Effect ◽  
Triacylglycerol Content ◽  
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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