Reaction rate studies of glucose-6-phosphate dehydrogenase activity in sections of rat liver using four tetrazolium salts

1985 ◽  
Vol 17 (9) ◽  
pp. 993-1008 ◽  
Author(s):  
R. G. Butcher ◽  
C. J. F. Van Noorden
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Reaction Rate ◽  
Tetrazolium Salts ◽  
Glucose 6 Phosphate Dehydrogenase

Maleimide as an inhibitor in measurement of erythrocyte glucose-6-phosphate dehydrogenase activity.

1978 ◽  
Vol 24 (6) ◽  
pp. 885-889 ◽  
Author(s):  
J Deutsch
Keyword(s):  
Dehydrogenase Activity ◽  
Coefficient Of Variation ◽  
Present Method ◽  
Reaction Rate ◽  
Hemoglobin Concentration ◽  
Statistical Correlation ◽  
Secondary Reaction ◽  
Phosphogluconate Dehydrogenase ◽  
Reagent Cost ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract Erythrocyte glucose-6-phosphate dehydrogenase activity is measured with a centrifugal analyzer by use of a commercial reagent kit and of the reaction glucose-6-phosphate + NADP+ leads to 6-phosphogluconolactone + NADPH. Rate of production of NADPH is measured and related to hemoglobin concentration. Maleimide is added to inhibit further production of NADPH in a secondary reaction by endogenous 6-phosphogluconate dehydrogenase. The method is compared with others that are designed to circumvent the secondary reaction by either (a) addition of excess phosphogluconate dehydrogenase to drive the secondary reaction to completion or (b) inhibition of endogenous phosphogluconate dehydrogenase by 2,3-diphosphoglycerate. The present method has the advantages that reaction rate more quickly becomes linear and reagent cost is less as compared with other methods. The within-run coefficient of variation was 3%. The various methods investigated showed good statistical correlation.

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.

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 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

scholarly journals Histochemical localization of NADP-dependent dehydrogenase activity with four different tetrazolium salts.

1984 ◽  
Vol 32 (9) ◽  
pp. 998-1004 ◽  
Author(s):  
C J Van Noorden ◽  
R G Butcher
Keyword(s):  
Dehydrogenase Activity ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Transport Systems ◽  
Electron Carrier ◽  
Tetrazolium Salts ◽  
Parenchymal Liver ◽  
Oxygen Sensitive ◽  
Parenchymal Cells ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Optimal Incubation

The properties of the four most commonly used tetrazolium salts, neotetrazolium, nitro blue tetrazolium (nitro-BT), tetranitro-BT, and 2-(2-benzothiazolyl-3-(4-phthalhydrazidyl)-5-styryl-te trazolium (BPST), have been compared for their effects on the localization of nicotinamide adenine dinucleotide phosphate (NADP)-dependent dehydrogenases under optimal incubation conditions in cryostat sections of rat liver. Glucose-6-phosphate dehydrogenase has been selected as an example of these dehydrogenases. It was found that the use of nitro-BT and tetranitro-BT, unlike neotetrazolium and BPST, in combination with an exogeneous electron carrier and azide, resulted in localization patterns in agreement with the sites of activity as determined by microchemical techniques. In the absence of an intermediate carrier the localization was very similar to that of NADPH cytochrome c (P450) reductase as demonstrated immunocytochemically. BPST did not properly localize dehydrogenase activity, most probably because of the redistribution of formazan, due to its lack of firm substantivity. Neotetrazolium reduction in nitrogen gave the localization pattern, both in the presence and absence of carrier, of the reductase, suggesting that the transfer of reducing equivalents from the exogenous electron carrier to neotetrazolium proceeds via cellular electron transport systems. The reduction of nitro-BT and tetranitro-BT via intermediate carriers was oxygen sensitive in parenchymal cells, but not in the non-parenchymal liver cells. This oxygen sensitivity could be blocked by azide. With neotetrazolium, oxygen inhibited both carrier-mediated and carrier-independent reactions, effects that were not reversed with azide. Possible mechanisms of action between oxygen, reduced carriers, and tetrazolium salts are discussed.

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