Allosteric inhibition of human liver aldehyde dehydrogenase by the isoflavone prunetin

1997 ◽  
Vol 53 (4) ◽  
pp. 471-478 ◽  
Author(s):  
Saifuddin Sheikh ◽  
Henry Weiner
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Allosteric Inhibition ◽  
Liver Aldehyde Dehydrogenase

scholarly journals The activation of aldehyde dehydrogenase by diethylstilboestrol and 2,2′-dithiodipyridine

1982 ◽  
Vol 207 (1) ◽  
pp. 81-89 ◽  
Author(s):  
T M Kitson
Keyword(s):  
Enzyme Activity ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Common Property ◽  
Rabbit Liver ◽  
Aldehyde Dehydrogenases ◽  
Cytoplasmic Enzyme ◽  
Sheep Liver ◽  
Low Concentrations ◽  
Liver Aldehyde Dehydrogenase

1. The activation of sheep liver cytoplasmic aldehyde dehydrogenase by diethylstilboestrol and by 2,2′-dithiodipyridine is described. The effects of the two modifiers are very similar with respect to variation with acetaldehyde concentration, pH and temperature. Thus the degree of activation is maximal when the enzyme is assayed at approx. 1 mM-acetaldehyde, is greater at 25 degrees C than at 37 degrees C, and is greater at pH 7.4 than at pH 9.75. With low concentrations of acetaldehyde both modifiers decrease the enzyme activity. 2. Diethylstilboestrol affects the sheep liver cytoplasmic enzyme in a very similar way to that previously described for a rabbit liver cytoplasmic enzyme. Preliminary experiments show that the same is true for a preparation of human liver aldehyde dehydrogenase. It is proposed that sensitivity to diethylstilboestrol (and steroids) is a common property of all mammalian cytoplasmic aldehyde dehydrogenases.

Spatial distribution of human liver aldehyde dehydrogenase isoenzymes

1999 ◽  
Vol 111 (6) ◽  
pp. 461-466 ◽  
Author(s):  
I. Piotr Maly ◽  
Valérie Crotet ◽  
D. Sasse
Keyword(s):  
Spatial Distribution ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Liver Aldehyde Dehydrogenase

Human liver aldehyde dehydrogenase: Subcellular distribution in alcoholics and nonalcoholics

Alcohol ◽  
1988 ◽  
Vol 5 (1) ◽  
pp. 73-80 ◽  
Author(s):  
D. Meier-Tackmann ◽  
G.C. Korenke ◽  
D.P. Agarwal ◽  
H. Werner Goedde
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Subcellular Distribution ◽  
Human Liver ◽  
Liver Aldehyde Dehydrogenase

Human liver aldehyde dehydrogenase: partial purification and properties

1969 ◽  
Vol 47 (3) ◽  
pp. 265-272 ◽  
Author(s):  
A. H. Blair ◽  
F. H. Bodley
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Deae Cellulose ◽  
Maximal Activity ◽  
Partial Purification ◽  
Aliphatic Aldehydes ◽  
Low Concentrations ◽  
Purification And Properties ◽  
Liver Aldehyde Dehydrogenase ◽  
Metabolic Reduction

Aldehyde dehydrogenase was partially purified from human liver. During purification, activity was resolved into one major and one minor species by DEAE-cellulose column chromatography; the properties of the predominant form were investigated.Aldehydes are oxidized when NAD+, but not NADP+, is the electron acceptor, maximal activity occurring between pH 9 and 10. Several aliphatic aldehydes and hydroxyaldehydes served as substrates for the enzyme. Benzaldehyde also was oxidized, but at a comparatively low rate. Aliphatic aldehydes carrying negatively charged groups are not oxidized. The enzyme is sensitive to low concentrations of two sulfhydryl reagents, p-chloromercuribenzoate and mercuric ions; this inhibition was reversed with sulfhydryl compounds. Like other aldehyde dehydrogenases, the human liver enzyme is inhibited by arsenite and the inhibition is potentiated by mercaptoethanol. Only 35% inhibition was produced by disulfiram at 40 μM; and diethyldithiocarbamate, its metabolic reduction product, had no effect on activity below 10 mM.

Bromoacetophenone as an affinity reagent for human liver aldehyde dehydrogenase

Biochemistry ◽  
1986 ◽  
Vol 25 (18) ◽  
pp. 5182-5189 ◽  
Author(s):  
Alexander D. MacKerell ◽  
Robert S. MacWright ◽  
Regina Pietruszko
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Affinity Reagent ◽  
Liver Aldehyde Dehydrogenase
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