Kinetics of Alcohol Dehydrogenase-Catalyzed Oxidation of Ethanol Followed by Visible Spectroscopy

2005 ◽  
Vol 82 (7) ◽  
pp. 1068 ◽  
Author(s):  
Kestutis Bendinskas ◽  
Christopher DiJiacomo ◽  
Allison Krill ◽  
Ed Vitz
Keyword(s):  
Alcohol Dehydrogenase ◽  
Visible Spectroscopy ◽  
Kinetics Of ◽  
Catalyzed Oxidation ◽  
Oxidation Of Ethanol

Biochemical aspects of the interaction of ethanol with barbiturates

1970 ◽  
Vol 48 (6) ◽  
pp. 706-711 ◽  
Author(s):  
H. Locksley Trenholm ◽  
William B. Maxwell ◽  
Charles J. Paul ◽  
G. Stuart Wiberg ◽  
Blake B. Coldwell
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzymatic Activity ◽  
Ammonium Sulfate ◽  
Hepatic Tissue ◽  
Alcohol Metabolism ◽  
Ammonium Sulfate Precipitation ◽  
Tissue Slices ◽  
Catalyzed Oxidation ◽  
Oxidation Of Ethanol

When pentobarbital is added to a hepatic supernatant enzyme fraction which contains alcohol dehydrogenase from a rat, the rates of the enzyme-catalyzed oxidation of ethanol and reduction of acetaldehyde are increased. The pentobarbital enhancement of enzymatic activity which is dependent on pentobarbital concentration is still observed when the enzyme is purified by column chromatography on DEAE- and CM-Sephadex and ammonium sulfate precipitation. In in vitro studies where hepatic tissue slices were incubated with alcohol, pentobarbital inhibited the metabolism of alcohol and increased the acetaldehyde levels in the incubation mixture. The addition of 32.5 mM NAD resulted in a return of alcohol metabolism and acetaldehyde concentrations to control levels.

scholarly journals Inhibition of microsomal oxidation of ethanol by pyrazole and 4-methylpyrazole in vitro Increased effectiveness after induction by pyrazole and 4-methylpyrazole

1986 ◽  
Vol 239 (3) ◽  
pp. 671-677 ◽  
Author(s):  
D E Feierman ◽  
A I Cederbaum
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ethanol Oxidation ◽  
Liver Microsomes ◽  
Chronic Ethanol ◽  
Ethanol Metabolism ◽  
Ethanol Treatment ◽  
Previously Treated ◽  
Kinetics Of ◽  
Oxidation Of Ethanol

Pyrazole and 4-methylpyrazole, which are inhibitors of alcohol dehydrogenase, were also found to be effective inhibitors of the oxidation of ethanol by liver microsomes (microsomal fractions) in vitro. Ethanol oxidation by microsomes from rats previously treated for 2 or 3 days with either pyrazole or 4-methylpyrazole appeared to be especially sensitive to inhibition in vitro by pyrazole or 4-methylpyrazole. The kinetics of inhibition by pyrazole or 4-methylpyrazole in all microsomal preparations were mixed, as the Km for ethanol was elevated while Vmax was lowered. However, Ki values for pyrazole (about 0.35 mM) and especially 4-methylpyrazole (about 0.03-0.10 mM) were much lower than those found with the saline controls (about 0.7-1.1 mM). In contrast, Ki values for dimethyl sulphoxide as an inhibitor of microsomal ethanol oxidation were similar in all microsomal preparations. Pyrazole and 4-methylpyrazole reacted with microsomes to produce type II spectral changes whose magnitude increased after treatment with either pyrazole or 4-methylpyrazole. Thus the increased inhibitory effectiveness of pyrazole and 4-methylpyrazole appears to be associated with increased interactions with the cytochrome P-450 isoenzyme(s) induced by these compounds. These isoenzymes have properties similar to those of the isoenzyme induced by chronic ethanol treatment. Therefore, caution is needed in the use of pyrazole or 4-methylpyrazole to assess pathways of ethanol metabolism, especially after chronic ethanol treatment, since these agents, besides inhibiting alcohol dehydrogenase, are also effective inhibitors of microsomal ethanol oxidation.

Iodoacetate inactivation of rape alcohol dehydrogenase

1980 ◽  
Vol 45 (5) ◽  
pp. 1601-1607 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová
Keyword(s):  
Alcohol Dehydrogenase ◽  
Protein Molecule ◽  
Sulfhydryl Groups ◽  
Inactivation Rate ◽  
First Order ◽  
Ph Dependent ◽  
Kinetics Of

Iodoacetate inactivates rape alcohol dehydrogenase (ADH, EC 1.1.1.1). The inactivation rate follows the kinetics of the first order, is pH-dependent, and decreases below pH 7.5. Besides irreversible alkylation of the sulfhydryl groups of the enzyme iodoacetate also forms a reversible complex with rape ADH. The coenzyme (NAD) and its analogs (ATP, ADP, AMP) competitively protect the enzyme against alkylation; o-phenanthroline also protects the enzyme against alkylation yet noncompetitively with respect to iodoacetate. Imidazole and o-phenanthroline compete with one another for binding to the protein molecule of rape ADH. Whereas o-phenanthroline decreases the inactivation rate imidazole increases the rate of iodoacetate inactivation.

scholarly journals Preparation and Assessment of Some Characteristics of Nanoparticles Based on Sodium Alginate, Chitosan, and Camellia chrysantha Polyphenols

2021 ◽  
Vol 2021 ◽  
pp. 1-11
Author(s):  
Phu Hoang Luong ◽  
Thuy Chinh Nguyen ◽  
The Dan Pham ◽  
Do Mai Trang Tran ◽  
Thi Ngoc Lien Ly ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Release Kinetics ◽  
Release Kinetic ◽  
Ionic Gelation ◽  
Visible Spectroscopy ◽  
Polyphenol Content ◽  
Release Process ◽  
Kinetics Of ◽  
Scanning Electron

This paper presents the characteristics, morphology, and properties of alginate/chitosan/polyphenol nanoparticles, in which polyphenols were extracted from Camellia chrysantha leaves collected in Tam Dao district, Vinh Phuc province (Vietnam). The alginate/chitosan/polyphenol nanoparticles were prepared by ionic gelation method at different polyphenol content. The characteristics and morphology of these nanoparticles were investigated using infrared spectroscopy (IR), ultraviolet-visible spectroscopy (UV-Vis), and scanning electron microscopy (SEM). Release kinetic of polyphenols from the alginate/chitosan/polyphenol nanoparticles was conducted in simulated human body fluids. The release kinetics of polyphenols from the above nanoparticles were also evaluated and discussed. The experimental results showed that the release process of polyphenols from the nanoparticles was dependent on three factors: time, pH of solution, and amount of polyphenols.

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 Thermodynamics and Molecular Kinetics of Liver Alcohol Dehydrogenase.

1963 ◽  
Vol 17 supl. ◽  
pp. 27-33 ◽  
Author(s):  
Keith Dalziel ◽  
Gad Yagil ◽  
Warren F. Diven ◽  
Mark Takahashi
Keyword(s):  
Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Kinetics Of
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