In Vivo Pharmacodynamic Studies of the Disulfiram Metabolite S-Methyl N,N-Diethylthiolcarbamate Sulfoxide:Inhibition of Liver Aldehyde Dehydrogenase

1994 ◽  
Vol 18 (2) ◽  
pp. 340-345 ◽  
Author(s):  
Bruce W. Hart ◽  
Morris D. Faiman
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Liver Aldehyde Dehydrogenase

scholarly journals Role of cytosolic rat liver aldehyde dehydrogenase in the oxidation of acetaldehyde during ethanol metabolism in vivo

1975 ◽  
Vol 152 (3) ◽  
pp. 709-712 ◽  
Author(s):  
C J Eriksson ◽  
M Marselos ◽  
T Koivula
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Oxidation Rate ◽  
Ethanol Metabolism ◽  
Minor Role ◽  
Liver Cytosol ◽  
A Minor ◽  
Liver Aldehyde Dehydrogenase ◽  
Phenobarbital Induction

The activity of a high-Km aldehyde dehydrogenase in the liver cytosol was increased by phenobarbital induction. No corresponding increase in the oxidation rate of acetaldehyde in vivo was found, and it is concluded that cytosolic aldehyde dehydrogenase plays only a minor role in the oxidation of acetaldehyde during ethanol metabolism.

scholarly journals Steady-state and pre-steady kinetic studies on mitochondrial sheep liver aldehyde dehydrogenase. A comparison with the cytoplasmic enzyme

1978 ◽  
Vol 171 (3) ◽  
pp. 527-531 ◽  
Author(s):  
A K H MacGibbon ◽  
L F Blackwell ◽  
P D Buckley
Keyword(s):  
Steady State ◽  
Aldehyde Dehydrogenase ◽  
Kinetic Studies ◽  
Kinetic Properties ◽  
Protein Fluorescence ◽  
Sheep Liver ◽  
Steady State Kinetic ◽  
Wide Range ◽  
Liver Aldehyde Dehydrogenase

Kinetic studies were carried out on mitochondrial aldehyde dehydrogenase (EC 1.2.1.3) isolated from sheep liver. Steady-state studies over a wide range of acetaldehyde concentrations gave a non-linear double-reciprocal plot. The dissociation of NADH from the enzyme was a biphasic process with decay constants 0.6s-1 and 0.09s-1. Pre-steady-state kinetic data with propionaldehyde as substrate could be fitted by using the same burst rate constant (12 +/- 3s-1) over a wide range of propionaldehyde concentrations. The quenching of protein fluorescence on the binding of NAD+ to the enzyme was used to estimate apparent rate constants for binding (2 × 10(4) litre.mol-1.s-1) and dissociation (4s-1). The kinetic properties of the mitochondrial enzyme, compared with those reported for the cytoplasmic aldehyde dehydrogenase from sheep liver, show significant differences, which may be important in the oxidation of aldehydes in vivo.

scholarly journals Aldehyde dehydrogenase in 2-acetaminofluorene-induced rat hepatomas. Ontogeny and evidence that the new isoenzymes are not due to normal gene de-repression

1977 ◽  
Vol 164 (1) ◽  
pp. 119-123 ◽  
Author(s):  
Ronald Lindahl
Keyword(s):  
Rat Liver ◽  
Aldehyde Dehydrogenase ◽  
Double Diffusion ◽  
Normal Liver ◽  
Normal Adult ◽  
Sprague Dawley ◽  
Adult Liver ◽  
Aldehyde Dehydrogenases ◽  
Adult Rat ◽  
Liver Aldehyde Dehydrogenase

The pre- and post-natal ontogeny of Sprague–Dawley rat liver aldehyde dehydrogenase [aldehyde–NAD(P)+ oxidoreductase, EC 1.2.1.5] is described. At no time in its ontogenetic development does normal liver aldehyde dehydrogenase exhibit any of the characteristics of a series of unique aldehyde dehydrogenases that can be isolated from 2-acetamidofluorene-induced rat hepatomas. Enzyme activity is first detectable in 15-day foetal liver and gradually increases throughout pre- and post-natal development until adult activities are attained by day 49 after birth. Electrophoretically, normal aldehyde dehydrogenase, throughout its ontogeny, exists as the same single isoenzyme found in normal adult liver. Isoelectric points for two normal liver isoenzymes demonstrable by isoelectric focusing are pH5.9 and 6.0. The immunochemical properties of aldehyde dehydrogenase during its ontogeny are identical with those of normal adult liver aldehyde dehydrogenase when tested against anti-(hepatoma aldehyde dehydrogenase) serum in Ouchterlony double-diffusion tests. The results indicate that the hepatoma-specific aldehyde dehydrogenases are not the result of the de-repression of genes normally repressed in adult rat liver or in some other adult tissue.

scholarly journals Horse Liver Aldehyde Dehydrogenase

1972 ◽  
Vol 247 (1) ◽  
pp. 260-266 ◽  
Author(s):  
Rhoda I. Feldman ◽  
Henry Weiner
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Horse Liver ◽  
Liver Aldehyde Dehydrogenase
Sign in / Sign up

Export Citation Format

Share Document