Alcoholic cardiomyopathy is characterized by impaired ventricular function although its toxic mechanism is unclear. This study examined the impact of cardiac overexpression of alcohol dehydrogenase (ADH), which oxidizes ethanol into acetaldehyde (ACA), on ethanol-induced cardiac contractile defect. Mechanical and intracellular Ca(2+) properties were evaluated in ventricular myocytes from ADH tr...

The kinetics of furfural inhibition of the enzymes alcohol dehydrogenase (ADH; EC 1.1.1.1), aldehyde dehydrogenase (AlDH; EC 1.2.1.5) and the pyruvate dehydrogenase (PDH) complex were studied in vitro. At a concentration of less than 2 mM furfural was found to decrease the activity of both PDH and AlDH by more than 90%, whereas the ADH activity decreased by less than 20% at the same concentrati...

The alcohol dehydrogenase (ADH’) of yeast has twice the molecular weight of the ADH of horse liver (l), contains 4 gm. atoms of zinc (2), and binds 4 moles of DPN per mole of protein (1). The liver ADH binds 2 moles of coenzyme per mole (3). These facts prompted the prediction that the liver ADH should contain 2 gm. atoms of zinc per mole of protein (2). The presence of 2 atoms of zinc in liver...

The alcohol dehydrogenase (ADH’) of yeast has twice the molecular weight of the ADH of horse liver (l), contains 4 gm. atoms of zinc (2), and binds 4 moles of DPN per mole of protein (1). The liver ADH binds 2 moles of coenzyme per mole (3). These facts prompted the prediction that the liver ADH should contain 2 gm. atoms of zinc per mole of protein (2). The presence of 2 atoms of zinc in liver...

The enzyme aldehyde dehydrogenase (ALDH) is essential for ethanol metabolism in mammals, converting the highly toxic intermediate acetaldehyde to acetate. The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehy...

Antibodies against human liver alcohol dehydrogenase (ADH) were produced in rabbits. Peroxidase-labeled protein-A with diaminobenzidine as substrate was used to detect anti-ADH binding in human tissue thin sections. In the kidney, ADH was localized in the epithelia of the tubuli; glomeruli and collecting tubules appeared negative. In prostata and epididymis, the epithelia stained strongly. In t...

Populations of Drosophila mojavensis from the deserts of the Baja California peninsula and mainland Mexico utilize different cactus hosts with different alcohol contents. The enzyme alcohol dehydrogenase (ADH) has been proposed to play an important role in the adaptation of Drosophila species to their environment. This study investigates the role of ADH in the adaptation of the cactophilic D. m...

Introduction Alcohol is readily distributed throughout the body in the aqueous blood stream after consumption as it is miscible in water. This paper critically evaluates and highlights the various aspects of alcohol metabolism and elucidates the role of Reactive oxygen species (ROS). Alcohol is rapidly absorbed in the bloodstream and metabolized primarily in the liver by the enzyme alcohol dehy...

Phylogenetic relationships and rates of nucleotide substitution were studied for alcohol dehydrogenase (ADH) genes by using DNA sequences from mammals and plants. Mammalian ADH sequences include the three class I genes and a class II gene from humans and one gene each from baboon, rat, and mouse. Plant sequences include two ADH genes each from maize and rice, three genes from barley, and one ge...

Human class I alcohol dehydrogenase (ADH) genes show developmental and tissue specific differences in expression at the polypeptide level. In these studies ADH expression was investigated at the RNA level. Northern blot analysis of total and poly (A) RNA from adult liver using pADH12 probe demonstrated multiple RNA size classes of 2.6, 2.2, 1.9 and 1.6kb. In contrast, fetal liver, and fetal int...