Kinetic ethylene glycol assay with use of yeast alcohol dehydrogenase.

1980 ◽  
Vol 26 (9) ◽  
pp. 1278-1280 ◽  
Author(s):  
J H Eckfeldt ◽  
R T Light
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ethylene Glycol ◽  
Trichloroacetic Acid ◽  
Reaction Rate ◽  
Kinetic Assay ◽  
Yeast Alcohol Dehydrogenase ◽  
Stable Temperature ◽  
Narrow Bandwidth ◽  
Ethylene Glycol Poisoning ◽  
Ethanol Determination

Abstract We describe a rapid, accurate, and precise two-point kinetic assay for ethylene glycol. The method involves use of a standard kit for ethanol determination with yeast alcohol dehydrogenase, and of a centrifugal analyzer. Alcohol dehydrogenase catalyzes the oxidation of ethylene glycol in a trichloroacetic acid-precipitated specimen; the resulting NADH production is monitored at 340 nm. The reaction rate is linear with concentration to 1.5 g of ethylene glycol per liter. Interference from methanol, ethanol, and isopropanol was easily recognized after a 30-min incubation at 100 degrees C. We believe that the method can be readily adaptable to any narrow-bandwidth, stable, temperature-controlled spectrophotometer and so should provide more widely for the prompt assessment of patients in whom ethylene glycol poisoning is suspected.

scholarly journals Subunit conformation of yeast alcohol dehydrogenase.

1978 ◽  
Vol 253 (23) ◽  
pp. 8414-8419
Author(s):  
H. Jörnvall ◽  
H. Eklund ◽  
C.I. Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase

Value of glycolic acid analysis in ethylene glycol poisoning: A clinical case report and systematic review of the literature

2018 ◽  
Vol 290 ◽  
pp. e9-e14 ◽  
Author(s):  
Gaspar Tuero ◽  
Jesús González ◽  
Laura Sahuquillo ◽  
Anna Freixa ◽  
Isabel Gomila ◽  
...  
Keyword(s):  
Systematic Review ◽  
Case Report ◽  
Ethylene Glycol ◽  
Glycolic Acid ◽  
Clinical Case ◽  
Review Of The Literature ◽  
Ethylene Glycol Poisoning

Two Fatal Cases of Ethylene Glycol Poisoning

1978 ◽  
Vol 18 (2) ◽  
pp. 102-107 ◽  
Author(s):  
D. A. L. Bowen ◽  
P.S. B. Minty ◽  
A. Sengupta
Keyword(s):  
Ethylene Glycol ◽  
Chromatographic Analysis ◽  
Gas Chromatographic Analysis ◽  
Ethylene Glycol Poisoning ◽  
Salient Features ◽  
Serum And Urine

Two cases of self poisoning by ethylene glycol are reported. The salient features of fatal acute ethylene glycol poisoning are mentioned with detailed histological and toxicological findings. Gas chromatographic analysis was used to determine ethylene glycol levels in serum and urine.

scholarly journals Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions

2003 ◽  
Vol 68 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rate Constants ◽  
Equilibrium Constants ◽  
Kinetic Mechanism ◽  
Yeast Alcohol Dehydrogenase ◽  
Catalyzed Reactions ◽  
The Individual ◽  
Individual Rate ◽  
Catalyzed Oxidation

In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25 ?C, have been estimated. The determination of the individual rate constants was achieved by fitting the reaction progress curves to the experimental data, using the procedures of the FITSIM and KINSIM software package of Carl Frieden. This work is the first report in the literature showing the internal equilibrium constants for the isomerization of the enzyme-NAD+ complex in yeast alcohol dehydrogenase-catalyzed reactions.

scholarly journals Binding of coenzymes to yeast alcohol dehydrogenase

2010 ◽  
Vol 75 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin ◽  
Mira Popovic ◽  
Julijan Kandrac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Equilibrium Constants ◽  
Point Mutations ◽  
Free Energies ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Mutant Type ◽  
Yeast Alcohol Dehydrogenase ◽  
Internal Equilibrium ◽  
Individual Reaction

In this work, the binding of coenzymes to yeast alcohol dehydrogenase (EC 1.1.1.1) were investigated. The main criterions were the change in the standard free energies for individual reaction steps, the internal equilibrium constants and the overall changes in the reaction free energies. The calculations were performed for the wild type enzyme at pH 6-9 and for 15 different mutant type enzymes, with single or double point mutations, at pH 7.3. The abundance of theoretical and experimental data enabled the binding of coenzymes to enzyme to be assessed in depth.

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