نتایج جستجو برای: adh alcohol dehydrogenase
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Alcohol dehydrogenase (ADH) is an enzyme in the human body that processes the alcohol concentration in the blood. Alcohol dehydrogenase is a dimer which means it’s a molecule that consists of two parts which are called monomers. There are seven different dehydrogenases. ADH can be found in many organisms and it facilitates the oxidisation of alcohols to aldehydes or ketones and at the same time...
The population of Trinidad and Tobago is composed mainly of people of East Indian (Indo-Trinidadians) and African (Afro-Trinidadians) ancestry. Differences in alcoholism rates exist between these two ethnic groups, and researchers have investigated whether these differences can be explained in part by variations in the genes encoding the alcohol-metabolizing enzymes alcohol dehydrogenase (ADH) ...
Butane-grown "Pseudomonas butanovora" expressed two soluble alcohol dehydrogenases (ADHs), an NAD(+)-dependent secondary ADH and an NAD(+)-independent primary ADH. Two additional NAD(+)-dependent secondary ADHs could be detected when cells were grown on 2-butanol and lactate. The inducible NAD(+)-independent 1-butanol dehydrogenase (BDH) of butane-grown cells was primarily responsible for 1-but...
The stage-specific expression of the Drosophila alcohol dehydrogenase (Adh) gene is achieved through the alternate activation of two tandem promoters. The proximal promoter is active primarily during late embryonic development and early larval stages, while the distal promoter is active in late third instar larvae and adults. Here, we provide evidence that this Adh promoter switch is regulated ...
In a recent study Drosophila larvae were injected with bacterial lipopolysaccharide (LPS) suspended in 1% ethanol and differentially induced protein fractions were identified. The levels of several proteins, including alcohol dehydrogenase (ADH), increased in LPS-treated flies and were labelled as immune response proteins. However, because control larvae were not injected with ethanol alone the...
Pyruvate decarboxylase (PDC, EC 4.1.1.1) and alcohol dehydrogenase (ADH, EC 1.1.1.1) are responsible for the anaerobic production of acetaldehyde and ethanol in higher plants. In developing soybean embryos, ADH activity increased upon imbibition and then declined exponentially with development, and was undetectable in leaves by 30 days after imbibition. PDC was not detectable in soybean leaves....
Sulfur mustard is a chemical warfare agent that causes blistering of the skin and damages the eyes and airway after environmental exposure. We have previously reported that thiodiglycol (TDG, 2,2'-bis-thiodiethanol), the hydrolysis product of sulfur mustard, is oxidized by alcohol dehydrogenase (ADH) purified from horse liver or present in mouse liver and human skin cytosol. Humans express four...
Chamberland V, Rioux P. Not only students can express alcohol dehydrogenase: goldfish can too! Adv Physiol Educ 34: 222–227, 2010; doi:10.1152/advan.00088.2009.—This article describes a novel approach to study the metabolic regulation of the respiratory system in vertebrates that suits physiology lessons for undergraduate students. It consists of an experimental demonstration of the goldfish’s ...
Fermentatively produced ethanol from lignocellulose by yeast is a renewable alternative to fossil fuels. However, inhibitors originating from the breakdown process of the raw material decrease the fermentation rate. Previous studies have made known inhibition effects by the furan compounds furfural and hydroxymethyl furfural (HMF). In the current work, the kinetics and inhibition effect of furf...
It is widely accepted that the Arabidopsis Adh (alcohol dehydrogenase) gene is constitutively expressed at low levels in the roots of young plants grown on agar media, and that the expression level is greatly induced by anoxic or hypoxic stresses. We questioned whether the agar medium itself created an anaerobic environment for the roots upon their growing into the gel. beta-Glucuronidase (GUS)...
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