• 제목/요약/키워드: acetaldehyde dehydrogenase

검색결과 126건 처리시간 0.031초

In vitro inhibition of 10-formyltetrahydrofolate dehydrogenase activity by acetaldehyde

  • Mun, Ju-Ae;Doh, Eun-Jin;Min, Hye-Sun
    • 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.

감과 가공식품의 알콜대사촉진물질 (Acetaldehyde Dehydrogenase Activator from Persimmon and Its Processed Foods)

  • 김석기;이영철;서광기;최혜선
    • 한국식품영양과학회지
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    • 제30권5호
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    • pp.954-958
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    • 2001
  • 감은 종기, 염증질환, 부스럼 화상을 치료하고 고혈압을 예방하고 동맥경화에 효과가 있고 숙취해소에 효능이 있다고 알려져있다. 감과육에 알콜대사에 관여하는 acetaldehyde dehydrogenase(ALDH)의 활성을 촉진하는 물질이 존재하므로ALDH의 활성을 촉진하는 물질을 감의 계절별, 품종별 측정을 했고 또 감을 이용한 가공식품에 농도를 측정하였다. ALDH의 활성을 촉진하는 물질은 부유의 경우 11월에 수확한 과일에서 가장 높고 품종별로는 부유가 가장 높았고 갑주백목은 부유와 유사하였고 청도반시, 서촌조생의 순이었다. 가공식품은 감건조품, 곶감, 감즙은 대체로 ALDH의 활성을 촉진하는 물질의 활성이 높게 유지되나 감음료, 감식초와 같은 음료는 ALDH의 활성을 촉진하는 물질의 활성이 낮았다. 감 자체뿐만 아니라 감가공식품에서도 ALDH의 활성을 촉진하는 물질의 활성이 어느 정도 유지되므로 이를 이용한 숙취해소작용이 기대된다.

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알데히드 탈수소 효소 활성에 미치는 글루타치온의 영향 (Effect of Glutathione on Aldehyde Dehydrogenase Activity)

  • 이은실;문전옥
    • Environmental Analysis Health and Toxicology
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    • 제16권1호
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    • pp.9-16
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    • 2001
  • It is known that alcoholics have significantly lower mitochondrial aldehyde dehydrogenase (ALDH)s'activity than do normal subjects or nonalcoholics with liver disease. However, there are only few reports that explain the reasons behind this reduction of ALDHs'activities. In this study, ALDH activity is inhibited by acetaldehyde, a substrate for ALDH However, the addition of glutathione (GSH) protected ALDH activities against the inhibitory effects of acetaldehyde in vitro. Furthermore, when GSH depletion is induced using diethyl maleate (DEM) in rats by 24% in cytosol and 43% in mitochondria, ALDH activities were also depressed by 31% and 63%, respectively compared to non-treated rats without significant reductions in other hepatic enzymes. These results suggest that ALDHs'activities are closely related to the concentration of acetaldehyde and/or cellular GSH contents . Therefore in alcoholic liver disease, increased productions of acetaldehyde and decreased contents of mitochondrial GSH may involved in the depression of ALDHs'activities.

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흰쥐에서 Acetaldehyde 대사에 미치는 복어추출물의 영향 (The Effect of Puffer Fish Extract on the Acetaldehyde Metabolism in Rat)

  • 김동훈;김동수;최종원
    • 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.

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Search for acetaldehyde trapping agents by using alcohol dehydrogenase assay

  • Lee, Hyun-Joo;Lee, Kang-Man
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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    • pp.160.3-161
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    • 2003
  • Aldehyde and active form of free oxygen produced in alcohol metabolism 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 P4502E1. Alcohol dehydrogenase is reversible in alcohol metabolism. To block the backward reaction and enhance alcohol oxidation, acetaldehyde trapping agents were assayed. The assay was carried out by measuring decreasing NADH at 340nm, using acetaldcehyde and NADH as substrate and coenzyme respectively. (omitted)

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바이오짐의 에탄올 대사에 대한 영향 (Effects of Biozyme on the Ethanol Metabolism in vivo and in vitro)

  • 남석우;박승희;윤성필;서동완;남태균;홍성렬;이향우
    • 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.

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Expression of Human Mitochondiral Aldehyde Dehydrogenase 2 in Mammalian Cells using Vaccinia Virus-T7 RNA Polymerase

  • Kang, Su-Min;Yoo, Seung-Ku;Lee, Ki-Hwan
    • 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.

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약용식물 추출물의 에탄올대사 효소활성에 미치는 영향 (Effect of Medicinal Plant Extracts on the Ethanol-Metabolizing Enzyme Activities)

  • 도재호;곽정원;이선정;노정진;이광승;김동청
    • 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.

Specificity of Alcohol Dehydrogenase from Clostridium acetobutylicum ATCC 4259

  • Kim, Byung-Hong;Zeikus, J.-Gregory
    • 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.

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정상인의 혈중 알코올 탈수소효소 활성도 및 에탄올, 아세트알데히드 농도에 관한 연구 (Activity of Alcohol Dehydrogenase and Ethanol, Acetaldehyde Levels in Normal Adults Blood)

  • 김기웅;양정선;이종성;조영숙;강성규;정호근
    • 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).

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