• Journal of Applied Biological Chemistry
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• v.65 no.3
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• pp.183-187
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• 2022

The hot water extract from cinnamon (Cinnamomum cassia Presl) inhibited the activity of alcohol dehydrogenase (ADH) with IC₅₀ value of 45.6 ㎍/mL. The ADH inhibitory components in cinnamon extract were relatively stable to acid and heat, but were found to be volatile. The optimum temperature and time for extracting the ADH inhibitory components from cinnamon were 80 ℃ and 2 h, respectively. Among the essential oils of cinnamon, cinnamaldehyde was the main substance for ADH inhibition. Cinnamaldehyde is considered a competitive inhibitor of ethanol to ADH. Therefore, the cinnamon extract and cinnamaldehyde showed the potential to be used as natural materials for relieving symptoms of a hangover.

• Preventive Nutrition and Food Science
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• v.6 no.4
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• pp.224-229
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• 2001

We investigated the effects of bean sprouts (Glycine max), dropwort (Oenanthe javanica), and radish (Raphanus sativus var. hortensis for. acanthiformis) extracts on alcohol dehydrogenase (ADH). The extracts from three kinds of vegetables were prepared by extracting with boiling water, distilling water, and ethyl alcohol. Among extracts, boiling water extract showed the highest activating effect on ADH, respectively and distilled water extract had a greater effect on ADH activation than that of alcohol extract. The ADH facilitating effect of bean sprout extract by distilled water was significantly higher than dropwort or radish, hut the effect of the bean sprout extract by ethyl alcohol was lower than others. The facilitating effect on ADH of mixture extracts of bean sprout and dropwort were mixed at 1 : 1 mixture of boiled-water extract showed the highest effectiveness. And bean sprout extract separated below 3000 molecular weight (MW) range of extract fraction had greater ADH activity than large MW parts.

• Analytical Science and Technology
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• v.12 no.6
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• pp.565-570
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• 1999

The alcohol dehydrogenase (ADH) gene from Bacillus stearothermopilus was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pGEX-KG, and expressed it as a fusion protein with glutathione S-transferase (GST) in E. coli. The recombinant ADH was produced by induction with 1 mM isopropyl-${\beta}$-D-thiogalactopyranoside at $37^{\circ}C$ and purified by glutathione affinity chromatography. The recombinant ADH exhibited high substrate specificity for ethanol. The activity of the recombinant ADH proceeded optimally at pH 9.0 and $70^{\circ}C$. The recombinant ADH was highly stable against high temperature. This thermostable alcohol dehydrogenase can be used for the enzymatic determination of alcohol and for the industrial production of alcohol.

• YAKHAK HOEJI
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• v.43 no.4
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• pp.481-486
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• 1999

Excessive or long term ingestion of alcohol may cause hepatitis, cirrhosis, hepatic tumor and so on. Aldehyde and active form of free oxygen that are metabolites of alcohol in liver are the cause of liver cell damage. The main system of alcohol metabolism is composed of alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH) and cytochrome P450. In connection with in vivo alcohol metabolism, more than one hundred natural products were screened for inhibition or activation of alcohol dehydrogenase. As a results, we found significant inhibition ($IC_50$) of ADH by methanolic extracts of Puerariae Radix ($61.2{\;}\mu\textrm{g}/ml$), Glycyrrhizae Radix ($105.0{\;}\mu\textrm{g}/ml$), Cinnamomi Ramulus ($7.0{\;}\mu\textrm{g}/ml$), Rhei Rhizoma ($36.7{\;}\mu\textrm{g}/ml$), Mori Cortex Radicis ($106.2{\;}\mu\textrm{g}/ml$), Chrysanthemi Flos ($112.2{\;}\mu\textrm{g}/ml$), Erycibes Caulis ($36.7{\;}\mu\textrm{g}/ml$), and Scutellariae Radix ($122.5{\;}\mu\textrm{g}/ml$)

• Korean Journal of Microbiology
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• v.37 no.3
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• pp.221-227
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• 2001

Heat shock proteins serve as chaperone by preventing the aggregation of denatured proteins and promote survival of pathogens in harsh environments. In bacteria, ethanol shock induced the major chaperone GroEL and DnaK, but in Streptococcus pneumoniae, it induced neither GroEL nor DnaK but alcohol dehydrogenase (ADH). In this study, ADH gene encoding a 104-kDa (p104) protein was identified and characterized. The deduced amino acid sequence of pneumococcal ADH shows homology with other members of the ADH family, and particularly with Entamoeba histolytica ADH2 and E. coli ADH. S. pneumoniae adh is composed of 883 amino acids and its estimated isoelectric point is 6.09. Although ADH is conserved between S. pneumoniae and E. coli, immunoblot analysis employing antisera raised against pneumococcus ADH demonstrated no cross-reactivity with ADH analog in Eschericha coli, Staphylococcus aureus and human HeLa cells. Also secretion of ADH was demonstrated by subcellular fractionation and immunoblot analysis of proteins. These results suggest that S. pneumoniae ADH could be a highly feasible candidate for both diagnostic marker and vaccine.

• Toxicological Research
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• v.14 no.4
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• pp.557-562
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• 1998

Allyl alcohol is metabolized in the liver through two steps, first to reactive acrolein by alcohol dehydrogenase (ADH), subsequently to acrylic acid by aldehyde dehydrogenase (ALDH). Since ethanol could compete the same enzymes to be metabolized in the liver, we have determined the plasma concentrations of allyl alcohol and ethanol followed by combined treatment. Pretreatment of rats with 2g/kg ethanol followed by ip administration of 40mg/kg allyl alcohol increased the lethality significantly. Determination of in vivo blood concentrations revealed that ethanol pretreatment caused the apparent decrease in allyl alcohol clearance, whereas acetaldehyde level in blood increased significantly by allyl alcohol treatment, as determined by head space GC analysis. Treatment of 4-methylpyrazole, an inhibitor of ADH, delayed allyl alcohol elimination significantly and reduced its lethality. Collectively, these findings suggested that reduction of allyl alcohol clearance in the presence oj ethanol was mediated through ADH competitive inhibition.

• International Journal of Industrial Entomology and Biomaterials
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• v.7 no.1
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• pp.51-57
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• 2003

A cDNA encoding a putative alcohol dehydrogenase (ADH) class III was cloned from the silkworm, Bombyx mono The full length cDNA is 1,385 nucleotides long and contains an open reading frame of 1,128 bp encoding 376 amino acid residues. The B. mon ADH III protein sequence was aligned with ADH III known from various organisms. Interestingly, the protein sequence of B. mon ADH III showed 87% and 85% identity to ADH III from marine fish Sparus aurata and Branchiostoma floridae, respectively, whereas rather low sequence identity (83%) to Drosophila melanogaster ADH III was observed. Northern blot analysis revealed that B. mon ADH III mRNA is expressed in all tissues from larva examined: fat body, midgut, epidermis, silk gland and ovary, with the highest level found in the fat body.

• YAKHAK HOEJI
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• v.38 no.2
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• pp.107-113
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• 1994

Ally alcohol is metabolized in the liver through two steps, first to reactive acrolein by alcohol dehydrogenase(ADH), subsequently to acrylic acid by aldehyde dehydrogenase(ALDH). Since ethanol could compete the same enzymes to be metabolized in the liver, we have studied the interaction between allyl alcohol and ethanol on liver toxicity. Simultaneous treatment of 2 g/kg ethanol by ip administration with 40 mg/kg allyl alcohol to rats increased the lethality significantly, accompanied by potentiation of the loss of hepatic glutathione. Collectively, these findings suggested that ethanol potentiated the hepatotoxicity and lethality induced by allyl alcohol probably through competing two metabolizing enzymes, ADH and ALDH.

• The Korean Journal of Zoology
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• v.22 no.2
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• pp.55-66
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• 1979

Drosophila melanogaster Oregon-R had been bred in a large quantity and the crude alcohol dehydrogenase (ADH) obtained was purified and the activity of the enzyme was measured, analyzed and its patterns were examined. The results obtained are presented below: 1. Through this experiment, it was found that the specific activity of ADH of the D. melanogaster is about more than five times as strong as that of the D. mlanogaster Samarkands which was found by Jacobson et al. in 1970. 2. It was learned that the ADH isozyme patterns of this strain was found to be $ADH_1$ and $AHD_2$ in the fast form and $ADH_5$ in the slow form. 3. It was learned that, $ADH_1, ADH_2$, and $ADH_5A$ are found as the ADH patterns of crude enzyme, and that $ADH_1, ADH_5A$ and $ADH_5B$ as the ADH patterns of the purified enzyme. 4. After the isolation andpurification of $ADH_5A$ and $ADH_1$ isozymes, specfic activity of $ADH_5A$ was found to be 4,330 (units/mg) and that of $ADH_1$ to be 3,670 (units/mg), and the exact position of their zymogram on the 7% acrylamide disc gel was distinguished.

• Food Engineering Progress
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• v.21 no.3
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• pp.286-291
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• 2017

This study was conducted to certify the effect of aqueous extracts from fifty medicinal plants on the activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in vitro. Each aqueous extract was prepared by combining one-part medicinal plants with twenty-parts distilled water at $80^{\circ}C$ for 8 h. Among the fifty medicinal plants, Allium sativum L. and Cinnamomum cassia Presl were regarded as an effective anti-hangover substance. Allium sativum L. extract increased ALDH activity more than 2 times compared with ADH activity, enhancing the acetaldehyde degradation. Cinnamomum cassia Presl extract dramatically inhibited ADH activity compared with ALDH activity, thus potently decreasing the acetaldehyde formation. ADH and ALDH activities were proportionally inhibited according to the increased concentration of Cinnamomum cassia Presl extract. The aqueous extract of Cinnamomum cassia Presl at a concentration of $45.33{\mu}g/mL$ inhibited ADH activity by 52.8% and ALDH activity by 11.0%.