• Journal of The Korean Society of Grassland and Forage Science
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• v.14 no.2
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• pp.82-87
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• 1994

This study was planned to identify the variety of Italian ryegrass using electrophoresis. Thirty seven varieties of Italian ryegrass were tested by starch gel electrophoresis. The specific electrophoretic zymograms of each variety were observed by Alcohol dehydrogenase(ADH) and Esterase. The results were surnrnerized as follows; 1. AU varieties displayed two band zones by ADH and Rf values were 0.63 and 0.6 (Table 2, Fig. 2). 2. There were five band type for ADH isozyme of 37 varieties classified with isozyme banding pattern. According to the isozyme band type 7, 2, 6, 18 and 4 varieties belong to group, I, II, III, IV, and V, respectively (Table 2). 3. The varieties displayed single band zone for Esterase isozyme and Rf value was 1.00 (Table 2, Fig. 4). 4. According to banding type, Esterase isozyme of 37 varieties classified into 3 groups, 22, 8 and 7 varieties belong to group, I , II, and III, respectively (Table 2).

• Natural Product Sciences
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• v.21 no.1
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• pp.54-58
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• 2015

The protective effect of EtOAc fraction of Limonium tetragonum extract (EALT) against alcohol-induced hepatotoxicity was assessed following acute ethanol intoxication in Spraque-Dawley rats. EALT (200 mg/kg p.o.) was administrated once before alcohol intake (8 g/kg, p.o.). Blood ethanol concentration, and the activities of alcohol metabolic enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the liver were measured. Also, the formation of malondialdehyde (MDA) and the activities of antioxidant enzymes, superoxide dismutase (SOD), glutathione peroxidase (GSH-px), catalase were determined after acute alcohol exposure. Pretreatment of rats received ethanol with EALT significantly decreased blood ethanol concentration and elevated the activities of ADH and ALDH in liver. The increased MDA level was decreased, and the reduced activities of SOD, GSH-px and catalase were markedly preserved by the treatment with EALT. This study suggests that EALT prevent hepatic injury induced by acute alcohol which is likely related to its modulation on the alcohol metabolism and antioxidant enzymes activities.

• Journal of the Korean Society of Food Science and Nutrition
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• v.43 no.9
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• pp.1363-1368
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• 2014

The physiological activities of cultivated Korean blue mussel (Mytilus edulis) and New Zealand green-lipped mussel (Perna canaliculus) were analyzed and compared. Both hot water extracts of blue mussel flesh (BMF) and green-lipped mussel flesh (GMF) showed increased activities of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH). BMF showed increased ADH and slightly decreased ALDH activities compared to GMF. 1,1-Diphenyl-2-picrylhydrazyl radical scavenging activity of BMF was higher than that of GMF at the same concentration. BMF and GMF showed similar inhibitory activity against angiotensin converting enzyme at a concentration of 30 mg/mL. These results suggest that cultivated Korean blue mussel has similar physiological activity with New Zealand green-lipped mussel.

• Applied Biological Chemistry
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• v.41 no.6
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• pp.447-450
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• 1998

Effects of organic solvents fraction from Ainsliaea acerifolia ethanol extract on alcohol metabolism in rats were examined and the results were as follows: Ethanol souble fraction, after a single oral administration to rats, was found to cause a significant decrease in the serum ethanol concentration as well as enhancement of liver cytosolic alcohol dehydrogenase(ADH) activity, on the other hand, the fraction insouble in ethanol was found to cause an increase ethanol concentration in the blood and inhibit ADH activity.

• Journal of Korean Society of Forest Science
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• v.68 no.1
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• pp.32-36
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• 1985

Megagametophyte tissues of Pinus densiflora were subjected to study the inheritance of acid phosphatase (ACP), alcohol dehydrogenase (ADH) and catalase (CAT) isozymes by starch gel zone-electrophoresis. At least three or four zones were segregated for ACP isozyme. However, as one isozyme of ACP-A zone was separated clearly, only that isozyme was analysed. Five isozyme phenotypes (A1-A5), observed in ACP-A zone, were segregated to a simple Mendelian ratio, suggesting that these are controlled by five codominant alleles existed at ACP-A locus. Two zones of activity were segregated in the gels after staining for ADH, the more anodal zone (ADH-A) of the two was invariant in our materials. Three isozyme phenotypes (B1-B3) were observed in ADH-B zone and these variants showed a 1:1 segregation pattern, suggesting that each variant is controlled by three codominant alleles at ADH-B locus. A total of five isozyme phenotypes, composed of multiple bands, were observed in CAT isozyme. The segregation of these phenotypes in heterozygous trees did not show any significant deviation from a 1:1 segregation. Therefore, the genetic control of CAT isozyme in Pinus densiflora seeds seems to be based on a single locus (CAT-A) with Five codominant alleles ($A_1-A_5$).

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.214-218
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• 2003

Alcohol consumption causes numerous consequences on the health of the human body. Heavy drinking on a daily base has caused liver diseases. Furthermore, some products such as acetaldehyde produced from alcohol metabolism are more toxic than alcohol itself. This study was carried out to evaluate the role of Lactobacillus casei on alcohol metabolism, especially, the removal of the toxic effect of alcohol. The maximum alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities from L. casei were observed at 4 hr of culture. L. casei was confirmed to produce the ADH and ALDH by the SDS-PAGE. From in vivo test using SD rats with 22% alcoholic drink, blood alcohol concentration (BAC), glutamic oxaloacetic transaminase (GOT) and glutamic pyruvic transaminase (GPT) of the rats feeding the medium containing L. casei were lower than those of the rats feeding the medium containing an alcoholic drink only This demonstrates that the ADH and ALDH produced by L. casei have virtual functions to detoxicate the alcohol in vivo and the fermentation broth of L. casei can be used as an alcohol detoxification drink.

• YAKHAK HOEJI
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• v.40 no.1
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• pp.78-83
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• 1996

An ethanol administration causes hepatic triglyceride accumulation in rats. To assess whether the herbal extract containing Phaseoli radiati semen(herbal extract) inhibit s the triglyceride accumulation in the liver, we determined the hepatic triglyceiide levels in rats fed ethanol and the herbal extract. In addition, the blood ethanol concentrations and the activities of hepatic alcohol dehydrogenase(ADH) and aldehyde dehydrogenase(ALDH) were measured to determine the effects of the herbal extract on alcohol metabolism in rats. The administration of the herbal extract markedly reduced the triglyceride levels elevated by ethanol in the liver as well as in the serum. The herbal extract remarkably lowered blood ethanol concentrations in a dose-dependent manner. The ADH activities decreased by ethanol were recovered to the normal level by the herbal extract treatment. Moreover, the ALDH activities slightly decreased by ethanol increased beyond the normal level by the herbal extract treatment. We conclude that the herbal extract inhibits the hepatic triglyceride accumulation and stimulates alcohol metabolism by preventing ADH and ALDH from inhbition by the ethanol administration in the rat liver.

• Food Science and Preservation
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• v.11 no.2
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• pp.201-206
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• 2004

The activities of antioxidation and alcohol dehydrogenase in hibitionin methanol extracts of thirty two medical herbs were tested using the method of DPPH activity, nitrite scavenging effect and alcohol dehydrogenase assay in vitro. In DPPH method, Eugenia caryophyllata, Thea sinensis, Paeonia suffruticosa, Alnus japonica showed over 90 % of free radical scavenging activities. The nitrite scavenging ability appeared Zanthoxylum bungeanum, Alnus japonica, Thea sinensis, Hovenia dulcis(cortex) and Illicium verum showed the high value. In connection with in vivo alcohol metabolism, thirteen medicinal herbs were screened for inhibition. As a reasult, we found significant inhibition of ADH by methanolic extracts of Glycyrrhiza uralensis, Pueraria thunbergiana(radix), Alnus japonica. These results indicate that the antioxidative effect was strongly related with alcohol dehydrogenase inhibitor; Thea sinensis and Alnus japonica.

• KSBB Journal
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• v.10 no.1
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• pp.30-37
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• 1995

Membrane-bound alcohol dehydrogenase(ADH) was purified to homogeneity from the acetic acid producing bacteria, Acetobacter sp. KM. The enzyme was solubilized and extracted with Triton X-100 and purified using the Mono-Q ion exchange chromatography and Superose 12 gel filtration chromatography. The enzyme was purified to 12-fold with a yield of 30%. The molecular weight of the purified enzyme was to be 335 KDa. SDS-PAGE of the enzyme showed two subunits with molecular weights of 79 KDa and 49 KDa. It indicated that the enzyme consisted of three subunits of the 79 KDa and two subunits of the 49 KDa. The purified .ADH preferentially oxidized straight chain aliphatic alcohol except methanol. Formaldehyde, acetaldehyde and glutaraldehyde were also oxidized. The apparent Km for ethanol was 1.04 mM and the optimum pH and temperature were 5.0∼6.0 and 32$^{\circ}C$, respectively. V2O5 and divalent cation such as ZnCl2 and NiCl2 inhibited enzymatic activity.

• KSBB Journal
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• v.31 no.2
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• pp.134-143
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• 2016

Lycii fructus has been traditionally used as a preventive and therapeutic medicine to treat enervation and diverse chronic diseases. In this study, we investigated whether fermentation of Lycii fructus extract (LE) increases the enzymatic activity of the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). The fermentation of LE by Bacillus subtilis subsp. subtilis and Saccharomyces cerevisiae IFO 2376 was shown to increase the enzymatic activity of ADH and ALDH. TLC analysis of LE and fermented LE (FLE) showed that ADH and ALDH activities increased in different spots. Fraction No. 66 of LE and fraction No. 68 of FLE by Silica gel chromatography showed increased ADH activity of 129.1% and 148.9%, respectively. Fractions No. 128 of LE and FLE by Silica gel chromatography showed increased ALDH activity of 134.1% and 148.1%, respectively. The fraction No. 68 of FLE obtained by HPLC showed new peaks at $R_t$ 11.938min, $R_t$ 22.072min and $R_t$ 28.842min, indicating that ADH activity was increased. The LE and FLE fractions with the greatest increases in ADH activity peaked at the same time ($R_t$ 13min),whereas the LE and FLE fractions with the greatest increases in ALDH activity peaked at different times ($R_t$ 16.307min and $R_t$ 36.640min, respectively).