Inhibition of liver aldehyde dehydrogenase by pyrogallol and related compounds

1975 ◽  
Vol 31 (4) ◽  
pp. 414-415 ◽  
Author(s):  
J. A. Rubenstein ◽  
M. A. Collins ◽  
B. Tabakoff
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Liver Aldehyde Dehydrogenase ◽  
Related Compounds

scholarly journals The action of chelating agents on human liver aldehyde dehydrogenase

1975 ◽  
Vol 151 (2) ◽  
pp. 443-445 ◽  
Author(s):  
R S Sidhu ◽  
A H Blair
Keyword(s):  
Binding Site ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Chelating Agents ◽  
Hydrophobic Interactions ◽  
Coenzyme Binding ◽  
Complexing Ability ◽  
Liver Aldehyde Dehydrogenase ◽  
Related Compounds ◽  
Coenzyme Binding Site

Human liver aldehyde dehydrogenase was inhibited by aromatic chelating agents. However, structurally related compounds with much lower metal-complexing ability displayed affinities for enzyme essentially equal to those of their respective chelating analogues. Inhibition was competitive with respect to the coenzyme. It is suggested that hydrophobic interactions between the inhibitors and the coenzyme-binding site of the enzyme are responsible for the observed effects on activity.

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

scholarly journals Horse Liver Aldehyde Dehydrogenase

1972 ◽  
Vol 247 (1) ◽  
pp. 267-272 ◽  
Author(s):  
Rhoda I. Feldman ◽  
Henry Weiner
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Horse Liver ◽  
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.

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