• Environmental Analysis Health and Toxicology
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• v.16 no.1
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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.

• 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 ($122.5{\;}\mu\textrm{g}/ml$)

• Journal of the Korean Chemical Society
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• v.45 no.1
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• pp.61-66
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• 2001

Stabilized Cross-linking Enzyme Crystals(CLEC) can be used as not only biocatalysts but also as enzyme sensors. PMS(Phenylmethyl Sulfate)was shown more efficience than any other electron mediator transfers toward HLADH(Horse Liver Alcohol Dehydrogenase)that were examined. NQS(naphtoquinonesulphonate), phenothiazine and ferrocene aldehyde had respectively just 52%, 37%, 35% electron transfer efficiency as compared to PMS . HLADH-CLEC was very stable toward elctron transfer mediators such as PMS, NQS and ferrocene aldehyde in which HLADH-solution was unstable.

• YAKHAK HOEJI
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• v.40 no.5
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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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• 2000.10a
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• pp.72-72
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• 2000

• Proceedings of the Korean Society of Applied Pharmacology
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• 1994.04a
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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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• v.11 no.6
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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.

• 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.

• 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.

• 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%.