Showing papers on "Aldehyde dehydrogenase published in 1968"
TL;DR: These experiments suggest a systematic relationship between the behavioral trait of ethanol preference and the activity of aldehyde dehydrogenase and a similar but much less pronounced relationship with alcohol dehydrogensase.
Abstract: Alcohol dehydrogenase and aldehyde dehydrogenase, the two principal enzymes of alcohol metabolism, were assayed in the livers of the inbred mouse strains C57BL/6J and DBA/2J. Previous work has shown that animals of various C57BL substrains prefer a 10% ethanol solution to water in a two-bottle preference test, and that animals of various DBA/2 substrains avoid alcohol. In the present study, C57BL/6J mice were found to have 300% more aldehyde dehydrogenase activity than DBA/2J mice and 30% more alcohol dehydrogenase activity. The F1 generation is intermediate to the parents in preference for the 10% alcohol solution and is also found to possess intermediate levels of alcohol and aldehyde dehydrogenase activity. These experiments suggest a systematic relationship between the behavioral trait of ethanol preference and the activity of aldehyde dehydrogenase and a similar but much less pronounced relationship with alcohol dehydrogenase.
96 citations
TL;DR: Kinetic studies with the partially purified enzyme suggest that decreased levels of NAD, such as occur after ethanol ingestion in vivo, would have a marked effect on enzyme activity, which may be important in oxidizing biologically active aldehydes derived from endogenous sources.
95 citations
TL;DR: Coenzyme A-linked aldehyde dehydrogenase from Escherichia coli strain B was purified 170-fold over cell-free extracts, and certain of its properties were investigated, suggesting the mechanism is "ping-pong".
83 citations
TL;DR: Whether the syndrome results from an accumulation of acetaldehyde due to a block in ethanol metabolism, or whether it is a result of an alteration in the metabolism of serotonin, the noncompetitive inhibition of aldehyde dehydrogenase by the sulfonylureas, coupled with the actions of ethanol, may be considered as a potential cause.
Abstract: The antabuse reaction, seen in patients imbibing alcohol while being treated with an antidiabetic sulfonylurea, is thought to be due to either an increase in acetaldehyde levels or an alteration in the metabolism of serotonin. Both can occur through an inhibition of aldehyde dehydrogenase. The oral antidiabetic sulfonylureas, chlorpropamide and tolbutamide, were found to be noncompetitive inhibitors of this enzyme. Acetaldehyde, a metabolite of ethanol, can competitively inhibit aldehyde dehydrogenase. Moreover, the oxidation of ethanol reverses the DPN/DPNH ratio so that the favored pathway of serotonin metabolism is altered, resulting in a decrease of 5-hydroxyindoleacetic acid (5-HIAA) and an increase of 5-hydroxytryptophol. Thus, ethanol augments the action of the sulfonylureas. Whether the syndrome results from an accumulation of acetaldehyde due to a block in ethanol metabolism, or whether it is a result of an alteration in the metabolism of serotonin, the noncompetitive inhibition of aldehyde dehydrogenase by the sulfonylureas, coupled with the actions of ethanol, may be considered as a potential cause.
53 citations
TL;DR: Homogeneous preparations of the potassium-requiring yeast aldehyde dehydrogenase are active with either DPN or TPN in the oxidation of a wide variety of aldehydes and may be reassociated to yield functional enzyme of higher molecular weight.
45 citations
TL;DR: The metabolism of 5‐hydroxyindoleacetaldehyde derived from 5-hydroxytryptamine incubated with tissue homogenates was studied as an indicator of aldehyde dehydrogenase and alcohol dehydrogenases activities.
Abstract: 1. The metabolism of 5-hydroxyindoleacetaldehyde derived from 5-hydroxytryptamine incubated with tissue homogenates was studied as an indicator of aldehyde dehydrogenase and alcohol dehydrogenase activities.2. In liver and brain from rats, there were indications of the presence of one or more aldehyde dehydrogenases which were stimulated by NAD(+) to a greater extent than by NADP(+).3. In liver from rats, there were indications of the presence of one or more alcohol dehydrogenases, which were stimulated by NADH to a greater extent than by NADPH.4. In brain from rats, there were indications of the presence of one or more alcohol dehydrogenases which were stimulated by NADPH to a greater extent than by NADH.
32 citations
TL;DR: The aldehyde dehydrogenase is protected effectively from iodoacetate inhibition, heat inactivation, and trypsin digestion when potassium and nicotinamide adenine dinucleotide are present and can be partly replaced by chelating agents.
29 citations
TL;DR: Reserpine activates rat microsomal monoamine oxidase to a greater extent than the mitochondrial enzyme and inhibits aldehyde dehydrogenase, which may account for the previously observed shift of urinary metabolite ratios after its administration.
29 citations
TL;DR: The reported ability of glyceraldehyde 3-phosphate dehydrogenase to act upon acetaldehyde and butyraldehyde is questioned on the basis of observations that these freshly distilled aldehydes are not substrates but become active as substrates when incubated in aqueous solutions.
20 citations
TL;DR: A study was made of serotonin-14C metabolism in rat liver homogenates with and without exogenous NAD and NADH, finding that neither ethanol nor disulfiram inhibited MAO and the aldehyde was converted to 5-hydroxytryptophol by the NADH-linked alcohol dehydrogenase.
15 citations
TL;DR: The generation of aldehydes and alcohols by the action of monoamine oxidase suggests that the deaminated metabolites of biogenic amines might exhibit some toxic effects in neuroblastoma patients.
Abstract: Neuroblastoma tumors, as well as cultured cells of neuroblastoma, contain high monoamine oxidase activity. The major deaminated metabolite of tyramine-H 3 in the incubation mixtures with the tumors or with the cultured cells is p- hydroxyphenylacetaldehyde. Upon addition of reduced nicotinamide-adenine dinucleotide phosphate, the aldehyde was further metabolized by the reductive pathway to p- hydroxyphenylethanol, whereas upon addition of nicotinamide-adenine dinucleotide phosphate the aldehyde was only metabolized to a minor extent by the oxidative pathway to p- hydroxyphenylacetic acid. Aldehyde dehydrogenase activity is very low in the neuroblastoma tumors and in the cultured neuroblastoma cells. The generation of aldehydes and alcohols by the action of monoamine oxidase suggests that the deaminated metabolites of biogenic amines might exhibit some toxic effects in neuroblastoma patients.
TL;DR: Aldehyde dehydrogenase was soluble below pH 4.0 but its sedimentation, diffusion, and viscosity behaviors indicated that it was denatured at low pH, to a subunit of molecular weight 95,000.
TL;DR: The results prove that the metabolism of fructose of the intestinal mucosa is the same as in liver and kidney and the transformation of fructose to glucose is rather poor during passage through the intestinal wall in rats.
TL;DR: Since alcohol dehydrogenase catalyses a reversible reaction, the distribution between oxidation and reduction of acetaldehyde was sensitive to the concentration ofanol; an increased concentration of ethanol reduced the formation of acetic acid.
Abstract: Acetaldehyde is an intermediate in alcoholic fermentation. The major part of it is reduced to ethanol but a minor fraction is normally oxidized to acetic acid. Owing to the kinetic properties of alcohol dehydrogenase and aldehyde dehydrogenase, the oxidized fraction decreased as the intracellular concentration was increased. Since alcohol dehydrogenase catalyses a reversible reaction, the distribution between oxidation and reduction of acetaldehyde was sensitive to the concentration of ethanol; an increased concentration of ethanol reduced the formation of acetic acid.