• 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.

• 약학회지
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• 제43권4호
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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 ($122.5{\;}\mu\textrm{g}/ml$)

• 대한화학회지
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• 제45권1호
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• pp.61-66
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• 2001

효소결정을 격자화하여 안정화한 CLEC은 생촉매제로써 뿐아니라 효소센서로 이용할 수 있다. 전자이동 중개체로 사용되고 있는 PMS는 HLADH에 대하여 가장 효율적인 전자이동 활성도를 가졌다. NQS는 PMS에 비하여 52%, phenothiazine은 37%, ferrocene aldehyde는 3 5%의 전자 이동 활성도를 가졌다. HLADH는 용액상태에서 PMS, NQS에 대하여 매우 불안정하였다. 반면에 HLADH-CLEC은 용액상태에서 불안정했던 PMS, NQS, ferrocene aldehyde에 대하여 매우 안정하였다.

• 약학회지
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• 제40권5호
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• pp.563-573
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• 1996

The system most likely responsible for the accelerated metabolism of alcohol with chronic ingestion or at high blood ethanol levels, is the microsomal ethanol-oxidizing system(M EOS). While the increase in the MEOS with chronic ethanol ingestion is thought to be adaptive, it may also have serious adverse effects on the liver. The rates of the NADPH-dependent oxygen consumption by the liver microsomes from the prolonged ethanol fed rats were 2 times higher than the rates from the non-treated rats. With the alcohol ingestion, the total SH and nonprotein SH contents showed the significant decrease and at the same time, MDA in liver and GOT and GPT levels in blood showed the significant increase, which suggests the occurrence of liver damage due to the oxidative stress caused by chronic alcohol consumption. The mitochondrial aldehyde dehydrogenase(ALDH) activity was decreased by chronic ethanol ingestion, whereas the alcohol dehydrogenase activity and the cytosolic ALDH activity were not altered. These results suggest that the induction of cytochrome P450 by the chronic alcohol ingestion increases the oxidative stress which seems to result in the altered the physiological states of the liver including the ALDH activity, which may in turn to lead to the liver disease.

• 대한예방의학회:학술대회논문집
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• 대한예방의학회 2000년도 제52차 추계학술대회 연제집
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• pp.72-72
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• 2000

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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• pp.323-323
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• 1994

Allyl alcohol은 간에서 두 단계의 효소 반응을 거쳐 대사되는데, 먼저, alcohol dehydrogenase (ADH)에 의해 독성 활성체인 acrolein으로 바뀌고, 이후 계속하여 aldehyde dehydrogenase (ALDH)에 의해 acrylic acid로 무독화되어 배설된다. Ethanol 역시 간에서 대사되는데 있어 같은 효소들을 공유하므로 allyl alcohol과 경쟁적으로 반응할 것이다. 따라서, 본 실험에서는 ethanol에 의한 대사 효소 경쟁반응에 의해 allyl alcohol 의 간독성이 어떻게 변화하는지를 연구하였다. 우선 ethanol과 allyl alcohol을 동시 투여할 경우 5시간째에 allyl alcohol에 의해 증가된 ALT level을 낮춘다는 보고를 확인하고자 ethanol 2 g/kg과 allyl alcohol 40 mg/kg을 동시투여했으나 오히려 치사율이 증가했고, ethanol을 2시간 전처리한 군에서도 역시 치사율이 증가되고, 간의 glutathione 양은 allyl alcohol 단독 처리군에 비해 현저히 감소되는 양상을 보였다.

• Journal of Microbiology and Biotechnology
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• 제11권6호
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• pp.928-933
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• 2001

Approximately 0.1 mg/ml of polyvinyl alcohol (PVA) was degraded by the growing cell, Brevibacillus laterospours, for 30 h, and 0.2 mg/ml of PVA was degraded by the cell-free extract that was isolated from Brevibacillus laterosporus. Approximately $0.29{\mu}g$/ml of acetic acid was produced from PVA by using the cell-free extract as a catalyst for 40 min. $V_{max}\;and\;K_m$ value of purified PAV-degradation enzyme was 3.75g/l and 2.75 g/l/min in reaction with EDTA and 3.99 g/l and 2.98 g/l/min in reaction without EDTA, respectively. Molecular weight of the purified enzyme determined by SDS-PAGE was 63,000 Da. Alcohol dehydrogenase and aldehyde dehydrogenase activities were qualitatively detected on a native acrylamide gel by an active staining method, indicating the existence of the metabolic pathway to use PVA as a substrate.

• 약학회지
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• 제38권2호
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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.

• 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.

• 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.