Showing papers on "Aldehyde dehydrogenase published in 1969"
TL;DR: Like other aldehyde dehydrogenases, the human liver enzyme is inhibited by arsenite and the inhibition is potentiated by mercaptoethanol, and the enzyme is sensitive to low concentrations of two sulfhydryl reagents.
Abstract: 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 properti...
138 citations
Journal Article•
TL;DR: Carboxytol butamide was formed from the oxidation of hydroxytolbutamide catalyzed by alcohol dehydrogenase and aldehyde dehydrogen enzyme, and the product of this reaction was oxidized by both xanthine oxidase andAldehyde dehydration.
Abstract: Incubation of tritiumlabeled tolbutamide with a 9000 x g rat liver supernatant resulted in a conversion to metabolically inactive carboxytolbutamide. The incubation of tolbutamide with rat liver microsomes resulted in the formation of hydroxytolbutamide. This conversion was inhibited by SKF 525-A. The oxidation of hydroxytolbutamide was carried out by the rat liver 100,000 x g supernatant. Alcohol dehydrogenase also catalyzed the oxidation of hydroxytolbutamide, and the product of this reaction was oxidized by both xanthine oxidase and aldehyde dehydrogenase. Carboxytolbutamide was formed from the oxidation of hydroxytolbutamide catalyzed by alcohol dehydrogenase and aldehyde dehydrogenase.
43 citations
TL;DR: The ethanol induced increase in plasma free fatty acid level, like that of alloxan diabetic and anti-insulin serum treated animals was significantly lowered following insulin injection, and the hepatic redox state was very much reduced.
Abstract: 1
Administration of insulin to normal fed male rats resulted in a significantly increased rate of ethanol oxidation by liver slices as compared to the control animals. The rate of ethanol oxidation by liver slices from alloxan diabetic and anti-insulin serum treated rats was significantly lower than normal.
2
Administration of ethanol to normal, insulin treated and alloxan diabetic animals caused a similar relative increase in the NADH/NAD ratio as measured by 4 different extra- and intramitochondrial redox pairs. After ethanol administration to alloxan diabetic rats, the hepatic redox state was very much reduced.
3
Intravenous injection of ethanol (1.5 g/kg body wt.) after 30 min resulted in significantly increased concentration of plasma free fatty acids. The ethanol induced increase in plasma free fatty acid level, like that of alloxan diabetic and anti-insulin serum treated animals was significantly lowered following insulin injection.
4
The total activities of hepatic alcohol dehydrogenase and aldehyde dehydrogenase were significantly decreased, after alloxan treatment. The enzyme activities in the insulin treated group were of the same magnitude as in control animals.
5
Partially purified rat liver alcohol dehydrogenase and aldehyde dehydrogenase were inhibited by free fatty acids. Laurate had a stronger inhibitory effect than palmitate and oleate. The inhibition of alcohol dehydrogenase was competitive with respect to alcohol and not with respect to NAD. The inhibition of aldehyde dehydrogenase was competitive with respect to aldehyde and not NAD.
6
Addition of laurate (0.8 mM) to liver slices caused a significant decrease in the ethanol oxidation rate.
27 citations
TL;DR: Results indicated that ethanol was utilized for lipid synthesis after being converted to acetyl-CoA via acetaldehyde viaacetaldehyde, and induction of aldehyde dehydrogenase was observed.
9 citations
TL;DR: These experiments suggest inhibition of hepatic aldehyde dehydrogenase, however, only weak in vitro inhibition was found and Deterring capabilities of metronidazole, butyraldoxime, and some other drugs for alcohol consumption were also analyzed in some studies.
Abstract: Publisher Summary This chapter focuses on studies of drug therapy for deterring alcohol intake in the chronic alcoholic. First advocated as a therapeutic aid in alcoholism in 1948, disulfiram continues to occupy a role as an adjunct to psycnotherapy and behavior therapy. It is generally accepted that disulfiram acts by blocking aldehyde dehydrogenase, causing a toxic elevation of circulating acetaldehyde when alcohol is consumed. The antidiabetic sulfonylureas, for example, chlorpropamide and tolbutamide, comprise another structural class which interacts with alcohol to produce a mild disulfiram-like reaction. Accumulation of acetaldehyde has been observed after tolbutamide and alcohol in man, and after chlorpropamide and alcohol in rats. Both sulfonylureas enhance the vasodepressor responses of exogenous acetaldehyde in cats, supporting the inference of decreased metabolism of acetaldehyde. These experiments suggest inhibition of hepatic aldehyde dehydrogenase, however, only weak in vitro inhibition was found. Deterring capabilities of metronidazole, butyraldoxime, and some other drugs for alcohol consumption were also analyzed in some studies.
6 citations
Journal Article•
5 citations
TL;DR: The aldehyde dehydrogenase activity in 21 species or strains of the genus Pseudomonas was determined in cell-free extracts prepared by a standard procedure, finding that none of the organisms possessed an aldealdehyde dehydrogenases activated by phosphate or arsenate, regardless of the degree of use of ethanol from the medium.
Abstract: The aldehyde dehydrogenase activity in 21 species or strains of the genus Pseudomonas was determined in cell-free extracts prepared by a standard procedure. Organisms grown in a salts – yeast extract – tryptone – ethanol medium all possessed an enzyme active on glycolaldehyde, using nicotinamide adenine dinucleotide (NAD+) as electron acceptor, which was activated by potassium ion. None of the organisms possessed an aldehyde dehydrogenase activated by phosphate or arsenate, regardless of the degree of use of ethanol from the medium.
4 citations