Determination of oxidized and reduced nicotinamide adenine dinucleotide in cell monolayers using a single extraction procedure and a spectrophotometric assay

2005 ◽  
Vol 338 (1) ◽  
pp. 131-135 ◽  
Author(s):  
Ken Umemura ◽  
Hideo Kimura
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Extraction Procedure ◽  
Spectrophotometric Assay ◽  
Nicotinamide Adenine ◽  
Single Extraction ◽  
Cell Monolayers ◽  
Reduced Nicotinamide Adenine Dinucleotide

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.

Residual Fluorescence as an Index of Purity of Reduced Nicotinamide Adenine Dinucleotide

1973 ◽  
Vol 19 (11) ◽  
pp. 1280-1284 ◽  
Author(s):  
Barbara F Howell ◽  
Sam Margolis ◽  
Robert Schaffer
Keyword(s):  
Alcohol Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Rate Of Reaction ◽  
Optical Rotations ◽  
Reduced Nicotinamide Adenine Dinucleotide

Abstract Determination of fluorescence remaining after reduced nicotinamide adenine dinucleotide (NADH) has reacted with excess acetaldehyde in the presence of alcohol dehydrogenase (EC 1.1.1.1) is useful as a criterion of NADH purity when used in conjunction with other methods for determining purity such as the rate of reaction, the ratio of ultraviolet absorbances at 260 nm and 340 nm, the color, and the chromatographic homogeneity of the preparation. Measurement of residual fluorescence monitors the enzymatically inactive material which absorbs at 340 nm. The specific optical rotations of NADH at several wavelengths are also reported.

Determination of LDH Isoenzymes

1966 ◽  
Vol 12 (11) ◽  
pp. 797-802 ◽  
Author(s):  
Julio Bergerman
Keyword(s):  
Cellulose Acetate ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Routine Procedure ◽  
Ldh Isoenzymes ◽  
Clinical Laboratories ◽  
Reduced Nicotinamide Adenine Dinucleotide

Abstract A method has been developed for the quantitation of LDH isoenzymes on cellulose acetate paper, taking advantage of the direct fluorometric procedures based on reduced nicotinamide adenine dinucleotide (NADH). The procedure is simple and the reagents relatively stable, allowing the test to become a routine procedure in clinical laboratories.

Sign in / Sign up

Export Citation Format

Share Document