• Nutrition Research and Practice
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• 제2권4호
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• pp.195-199
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• 2008

Alcoholism has been associated with folate deficiency in humans and laboratory animals. Previous study showed that ethanol feeding reduces the dehydrogenase and hydrolase activity of 10-formyltetrahydrofolate dehydrogenase (FDH) in rat liver. Hepatic ethanol metabolism generates acetaldehyde and acetate. The mechanisms by which ethanol and its metabolites produce toxicity within the liver cells are unknown. We purified FDH from rat liver and investigated the effect of ethanol, acetaldehyde and acetate on the enzyme in vitro. Hepatic FDH activity was not reduced by ethanol or acetate directly. However, acetaldehyde was observed to reduce the dehydrogenase activity of FDH in a dose- and time-dependent manner with an apparent $IC_{50}$ of 4 mM, while the hydrolase activity of FDH was not affected by acetaldehyde in vitro. These results suggest that the inhibition of hepatic FDH dehydrogenase activity induced by acetadehyde may play a role in ethanol toxicity.

• 한국식품영양과학회지
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• 제23권2호
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• pp.187-191
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• 1994

The present stduy was undertaken to investigate the possible effect of Puffer fish skin extract (Pf) on the heptic acetaldehyde metabolism . It was obsrved that PF markedly decreased the acetaldehyde levels in blood and liver. The activity of mitochondrial aldehyde dehydrogenase (Ald DH) increased by induction of acute intoxicatiion of alcohol (5 g/kg) was further increased through pretreatment with PF for 2 weeks. When PF was given to rat fed with 25% alcohol solution instead of water for 6 weeks. the activity of Ald DH in mitochondrial fraction decreased to about 28% compared with sucrose-treated group. But after pretreatemnt of PF, the activity was restored to the normal level. By the treatment with disulfiram (300 mg/kg, once a day for 3days) was restored to the control after the pretreatment with PF. And also mitochondrial Ald DH activity in vitro was not changed. All these observations suggest that reduction of acetaldehyde levels are partly due to increase activity of mitochondrial Ald DH. Therefore, the recovery from intoxication of acetaldehyde may be enhanced by treatment with PF.

• Biomolecules & Therapeutics
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• 제3권2호
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• pp.171-175
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• 1995

Effects of $Biozyme_{R}$ and $\textrm{Business}_{R}$ on alcohol metabolism in rats, and on the activities of alcohol dehydrogenase(ADH) and acetaldehyde dehydrogenase(ALDH) were studied in vitro. Alcohol concentration in rat blood was decreased after the treatment of Business(3.3 mι/kg, Biozyme 1.67 mg/wι) and Biozyme(3.3 mι/kg, 1.67 mg/mι) prior to the administration of ethanol(25%, 0.83 g/kg). And the acetaldehyde concentration of rat blood was also decreased when compared with control values in the same condition. Effects of Biozyme on ADH and ALDH activity were also studied. While the ALDH activity was elevated in the presence of Biozyme(2 $\mu\textrm{g}$/assay), the ADH activity was not influenced by Biozyme at the concentration range from 2 $\mu\textrm{g}$/assay to 0.2 mg/assay. In summary, Biozyme accelerated the rate of ethanol metabolism and the acceleration might be due to the increase in ALDH activity.vity.

• Journal of Microbiology
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• 제37권1호
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• pp.41-44
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• 1999

Human mitochondrial aldehyde dehydrogenase 2 (ALDH2) is mainly responsible for oxidation of acetaldehyde generated during alcohol oxidation in vivo. A full-length cDNA of human liver ALDH2 was successfully expressed using a vaccinia virus-T7 RNA polymerase system. The expressed ALDH2 had an enzymatic activity as high as the native human liver ALDH2 enzyme.

• 산업식품공학
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• 제21권3호
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• pp.286-291
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• 2017

약용식물의 열수 추출물이 in vitro에서 alcohol dehydrogenase (ADH)와 aldehyde dehydrogenase (ALDH)의 활성에 미치는 영향을 확인하였다. 약용식물에 20배의 증류수를 넣고 $80^{\circ}C$에서 8시간 추출하여 얻어진 추출액을 시료로 사용하였다. 50종의 약용식물 중에서 마늘과 육계 추출물이 숙취해소 천연소재로서의 활용 가능성이 가장 높게 나타났다. 마늘 추출물은 ADH에 비해 ALDH의 활성을 2배 이상 촉진시킴으로써 acetaldehyde의 분해가 잘 되게 하였다. 육계 추출물은 ALDH의 활성에 비해 ADH의 활성을 획기적으로 저해함으로써 acetaldehyde의 생성을 크게 억제하였다. 육계 추출물은 농도에 비례하여 ADH와 ALDH의 활성을 저해하였으며, $45.33{\mu}g/mL$의 농도에서 ADH의 활성을 52.8% 저해하였고 ALDH의 활성을 11.0% 저해하였다.

• Journal of Microbiology and Biotechnology
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• 제2권4호
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• pp.268-272
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• 1992

Alcohol dehydrogenase activity of Clostridium acetobutylicum ATCC 4259 was studied for its specificity against substrates in acidogenic and solventogenic cultures. The bacterium reduces propionate, valerate and caproate added to the medium to the corresponding alcohols. Acetaldehyde, propionaldehyde, butyraldhyde, pentanal, and hexanal were used as the substrates by alcohol dehydrogenase, and all were reduced to the corresponding alcohols with varying affinities and reaction velocities. Acetaldehyde showed the lowest affinity and lowest velocity while the other aldehydes showed similar $K_m\;and\;V_max$ values. NADPH was used as the electron donor for the reduction of aldehydes. Alcohol dehydrogenase activity was low in acidogenic culture, and high in solventogenic culture.

• 한국산업보건학회지
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• 제4권2호
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• pp.240-247
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• 1994

To identify normal levels of ethanol, acetaldehyde and alcohol dehydrogenase(ADH) activity in blood of Koreans, ethanol and acetaldehyde levels, activity of ADH in blood of Koreans, ethanol and acetaldehyde levels, activity of ADH in blood were measured in 97 subjects(male : 36, female : 61), 45 subjects(male : 21, female : 24) were not exposed to organic solvents and any other chemicals. Fifty two subjects(male : 15, female : 37) were exposed to organic solvents including toluene and xylene. The results were summerized as follows : 1. The blood ADH was not detected in exposed and non-exposed group. 2. The average blood ethanol level of non-exposed group was 0.0490 mg/dl, and exposed group was 0.0363 mg/dl. They were statistically significant(p<0.05). 3. The blood acetaldehyde levels in exposed group were significantly higher than that of non-exposed group was not statistically significant (p>0.05). 4. The average blood ethanol level of males in both groups was significantly higher than that of females, however, they were not statistically significant (p>0.05).

• 생물정신의학
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• 제31권1호
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• pp.1-6
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• 2024

Objectives Alcohol is metabolized to acetaldehyde by alcohol dehydrogenase enzyme in the liver and then acetaldehyde is metabolized to acetone by aldehyde dehydrogenase (ALDH) in the liver. There are two main ALDH enzymes which metabolize the acetaldehyde produced during ethanol oxidation. In particular, in the presence of the ALDH2 1^*2 allele, the activity of the ALDH 2 enzyme is lowered. As a result, acetaldehyde metabolism is slowed down and acetaldehyde accumulates in the body compared to the ALDH2 1^*1 allele. There are many studies that have investigated the blood acetaldehyde concentration according to the ALDH2 genotype, but there are few studies to compare this with age. So we investigated the blood acetaldehyde concentration according to ALDH2 genotype, age and gender. Methods According to the ALDH2 genotype, we divided the group by gender and age. We divided the age group in to three groups which ranged from 20 to 34 years old, from 35 to 49 years old, and lastly from 50 to 64 years old. And then we collected blood samples after 15 min, 30 min, 1 hr, 2 hr, 3 hr, 4 hr, 5 hr and 15 hr of after drinking to measure the blood acetaldehyde concentration. Results In ALDH2 1^*2 allele group, there are significant differences of the blood acetaldehyde concentration between the age groups. In ALDH2 1^*2 allele and male group, there are significant differences of the blood acetaldehyde concentration between the age groups. Conclusions There are significant differences of the blood acetaldehyde concentration between the age groups according to ALDH2 genotype. Also, there are significant differences of the blood acetaldehyde concentration between the age groups with male gender and ALDH2 1^*2 allele. Studies about other factors that may influence the blood acetaldehyde concentration are needed.

• Natural Product Sciences
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• 제21권2호
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• pp.98-103
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• 2015

Pueraiae Radix (PR), Pueratia Folium (PF) and Sorbus commixta (SC) mixture, namely GS-SP (PR (1)/PF (2)/SC (0.5): v/v/v) was developed as hangover-relieving elixir and its effects on alcoholic metabolism have been investigated. The enzymatic activity of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) of GS-SP was shown higher than those of single treatment with PR, PL, SC, and the positive control group (YM-808). The survival rate of mouse liver cell line NCTC clone 1469 in the presence of acetaldehyde was 30.6, 22.2, and 8.7% at the GS-SP dosage level of 50, 100, and 200 μg/mL respectively. Different concentrations of 50, 100 and 200 mg/kg of GS-SP showed efficient activity for ADH and ALDH than YM-808 in rat fed with 25% ethanol. The levels of blood alcohol and acetaldehyde after oral administration of 200 mg/kg of GS-SP showed efficient activity of 11.7% and 37% than those of YM-808. These results have been supported to the potential for GS-SP to serve as an excellent potential in providing hangover relief and liver protection.

• Toxicological Research
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• 제14권4호
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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.