نتایج جستجو برای: adh alcohol dehydrogenase
تعداد نتایج: 185772 فیلتر نتایج به سال:
Poisonings from toxic alcohols, such as methanol (MeOH) are a serious toxicological concern worldwide. In an endemic methanol poisoning in 2012 in the Czech Republic 121 subjects had consumed adulterated beverages and 41 died from the poisoning. An additional 20 subjects still suffer from visual/CNS sequelae [1]. In addition to mass poisonings single cases of methanol poisoning had been publish...
Extracts from benzyl-alcohol-grown Rhodococcus erythropolis DSM 1069 showed NAD(P)-independent, N,N-dimethyl-4-nitrosoaniline (NDMA)-dependent alcohol dehydrogenase activity. The enzyme exhibiting this activity was purified to homogeneity and characterized. It appears to be a typical nicotinoprotein as it contains tightly bound NADH acting as cofactor instead of coenzyme. Other characteristics ...
Rat liver cytosolic alcohol dehydrogenase (ADH) is the principal enzyme which catalyzes the oxidation of ethanol. ADH activity is known to be significantly higher in females than in males. However, the precise mechanism of the sex-difference in ADH activity is uncertain. Recently, we have shown that the inhibitory action of androgen and the slight facilitatory actions of progestin and estrogen ...
In vivo levels of enzymatic activity may be increased through either structural or regulatory changes. Here we use Drosophila melanogaster alcohol dehydrogenase (ADH) in an experimental test for selective differences between these two mechanisms. The well-known ADH-Slow (S)/Fast (F) amino acid replacement leads to a twofold increase in activity by increasing the catalytic efficiency of the enzy...
cDNAs for alcohol dehydrogenase (ADH) isozymes were cloned and sequenced from two tephritid fruit flies, the medfly Ceratitis capitata and the olive fly Bactrocera oleae. Because of the high sequence divergence compared with the Drosophila sequences, the medfly cDNAs were cloned using sequence information from the purified proteins, and the olive fly cDNAs were cloned by functional complementat...
Alcohol dehydrogenase (ADH) participates in the formation of retinoic acid from retinol in various organs including the gastric mucosa. However, its clinical significance still remains to be clarified. In this study, we identified the ADH isoforms responsible for the retinoic acid formation among various ADH isoforms, and examined associations among the ADH activities, the retinoic acid formati...
We have sequenced 4 kb of the genomic region comprising the Adh (Alcohol dehydrogenase) gene of Drosophila subobscura. In agreement with other species which belong to the same subgenus, two structural genes, Adh and Adh-dup, are contained in this region. The main features of these two genes of D. subobscura have been inferred from the sequence data and compared with the homologous region of D. ...
The catalytic reduction of renewable furfural into furfuryl alcohol for various applications is in the ascendant. Nonetheless, conventional chemo-catalysis hydrogenation always suffers from poor selectivity, harsh conditions, and expensive catalysts. Herein, to overcome serious technical barriers production, an alternative bio-electrocatalytic system was established under mild neutral where dis...
Ethanol containing beverages (alcoholic beverages) are socially acceptable that expected to provide refreshment, satisfaction and stress relief. Common types of ethanol include: wine, beer, syrup. According the World Health Organization, alcohol abuse is a risk factor for high mortality many diseases in humans such as fatty liver, hepatomegaly, cirrhosis, liver cancer, larynx nasopharynx stomac...
An alcohol dehydrogenase (ADH) gene from Clostridium acetobutylicum was cloned on a recombinant plasmid, pCADH100. Escherichia coli HB101, and an allyl alcohol-resistant mutant, HB101-adh1, containing this plasmid were unable to grow aerobically or anaerobically on agar media containing sublethal concentrations of allyl alcohol. E. coli HB101 and HB101-adh1 transformed with the plasmid pCADH100...
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