Potentiometric determination of nicotinamide adenine dinucleotide phosphate and glutathione reductase

1982 ◽  
Vol 54 (2) ◽  
pp. 303-307 ◽  
Author(s):  
Saad S. M. Hassan ◽  
G. A. Rechnitz
Keyword(s):  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Potentiometric Determination

scholarly journals DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN MICROGRAM SAMPLES OF TISSUE, QUANTITATIVE HISTOLOGIC DISTRIBUTION OF THE ENZYME IN THE RAT ADRENAL AND EFFECT OF ADRENOCORTICOTROPIN

1968 ◽  
Vol 16 (3) ◽  
pp. 185-190 ◽  
Author(s):  
NORBERTO A. SCHOR ◽  
DAVID GLICK
Keyword(s):  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Reductase Activity ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Border Region ◽  
Nicotinamide Adenine ◽  
Subcutaneous Injections ◽  
Glutathione Reductase Activity ◽  
Reduced Nicotinamide Adenine Dinucleotide

A fluorometric method for determination of glutathione reductase activity in microgram samples of tissue, i.e., microtome sections, based on measurement of the decrease of reduced nicotinamide adenine dinucleotide phosphate due to its oxidation on reaction with oxidized glutathione, was developed and applied to the quantitative histologic distribution of the enzyme in the adrenal gland of the rat. Single subcutaneous injections of adrenocorticotropin in saline solution (25 mg/kg) produced little change of enzyme activity in any of the histologic zones, although there was some tendency for the peak activity to shift from fasciculata to the fascicular-reticular border region. The possible interrelationship of glutathione reductase with ascorbic acid and reduced nicotinamide adenine dinucleotide phosphate in adrenal function was considered.

Enzymatic-Ultraviolet Determination of Glucose and Fructose in Wine: Collaborative Study

1985 ◽  
Vol 68 (5) ◽  
pp. 1021-1024 ◽  
Author(s):  
Guenther Henniger ◽  
Leonard Mascaro
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Collaborative Study ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Phosphoglucose Isomerase ◽  
Nicotinamide Adenine ◽  
Matched Pairs ◽  
Repeatability And Reproducibility ◽  
Standard Deviations ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract This collaborative study on the determination of glucose and fructose in wine was performed by 18 laboratories on 4 matched pairs of commercial wine. The method uses the enzymes hexokinase, glucose-6- phosphate dehydrogenase, and phosphoglucose isomerase and the coenzyme nicotinamide-adenine dinucleotide phosphate. Both glucose and fructose can be determined in the same sample without separation. The method is simple but care is necessary to ensure precise transfer of small volumes. Repeatability and reproducibility standard deviations for glucose ranged from 2.6 to 14.6 mg/L and 4.7 to 16.5 mg/L, respectively. Repeatability and reproducibility values for fructose ranged from 2.4 to 16.1 mg/L and 6.0 to 21.3 mg/L, respectively. The method has been adopted official first action

scholarly journals CYTOCHEMICAL DEMONSTRATION OF GLUTATHIONE REDUCTASE (EC 1.6.4.2) IN SACCHAROMYCES CEREVISIAE

1967 ◽  
Vol 15 (5) ◽  
pp. 273-275 ◽  
Author(s):  
JÜRGEN REISS
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Reduced Glutathione ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Yeast Cells ◽  
Nicotinamide Adenine ◽  
Cytochemical Demonstration ◽  
Ph Level ◽  
Essential Prerequisite

A method for the cytochemical demonstration of glutathione reductase in unfixed yeast cells ( Saccharomyces cerevisiae) is described using reduced glutathione as substrate, nicotinamide adenine dinucleotide phosphate (nicotinamide adenine dinucleotide) as coenzyme and nitro blue tetrazolium as indicator. An essential prerequisite is an exactly controlled pH level (pH 6.5) of the complete incubation medium.

Extracellular glutathione inhibits oxygen-induced permeability changes in alveolar epithelial monolayers

2001 ◽  
Vol 91 (2) ◽  
pp. 748-754 ◽  
Author(s):  
J. H. Roum ◽  
A. S. Aledia ◽  
L. A. Carungcong ◽  
K.-J. Kim ◽  
Z. Borok
Keyword(s):  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Clinical Manifestations ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Alveolar Epithelium ◽  
Oxygen Toxicity ◽  
Nicotinamide Adenine ◽  
Protective Effects ◽  
Alveolar Epithelial ◽  
Active Ion Transport

Exposure to high fractional inspired oxygen for 24 h increases permeability of the alveolar epithelium, contributing to the clinical manifestations of oxygen toxicity. Utilizing a model of the alveolar epithelium in which isolated rat type II cells form polarized monolayers on polycarbonate filters [transepithelial resistance ( R t) > 1 kΩ · cm2 by day 4], we evaluated the ability of reduced glutathione (GSH) to ameliorate these changes. On day 4, apical fluid was replaced with culture medium containing 1) no additives, 2) GSH (500 μM), or 3) GSH (500 μM) + glutathione reductase (0.5 U/ml) + nicotinamide adenine dinucleotide phosphate (250 μM). Monolayers were exposed (for 24 h) to room air (control) or 95% O2, each containing 5% CO2. After 24 h of hyperoxia, R t for condition 1decreased by 45% compared with control ( P < 0.001). In conditions 2 and 3, R tdid not decrease significantly ( P = not significant). Hyperoxia-induced decreases in active ion transport were observed for conditions 1 and 2 ( P < 0.05), but not for condition 3 ( P = not significant). These findings indicate that extracellular GSH may protect the alveolar epithelium against hyperoxia-induced injury. Addition of glutathione reductase and nicotinamide adenine dinucleotide phosphate may further augment these protective effects of GSH.

Effect of Niacin on Mitochondria of Allium Cepa Root Cells

1967 ◽  
Vol 25 ◽  
pp. 78-79
Author(s):  
M. Arif Hayat
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Hydrogen Transfer ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Root Tips ◽  
Root Cells ◽  
Transfer Processes ◽  
Standard Procedures ◽  
A Cell ◽  
Critical Interest

Although it is recognized that niacin (pyridine-3-carboxylic acid), incorporated as the amide in nicotinamide adenine dinucleotide (NAD) or in nicotinamide adenine dinucleotide phosphate (NADP), is a cofactor in hydrogen transfer in numerous enzyme reactions in all organisms studied, virtually no information is available on the effect of this vitamin on a cell at the submicroscopic level. Since mitochondria act as sites for many hydrogen transfer processes, the possible response of mitochondria to niacin treatment is, therefore, of critical interest.Onion bulbs were placed on vials filled with double distilled water in the dark at 25°C. After two days the bulbs and newly developed root system were transferred to vials containing 0.1% niacin. Root tips were collected at ¼, ½, 1, 2, 4, and 8 hr. intervals after treatment. The tissues were fixed in glutaraldehyde-OsO4 as well as in 2% KMnO4 according to standard procedures. In both cases, the tissues were dehydrated in an acetone series and embedded in Reynolds' lead citrate for 3-10 minutes.

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