• Title/Summary/Keyword: alcohol dehydrogenase(ADH)

Search Result 220, Processing Time 0.024 seconds

Characterization and Expression of Chironomus riparius Alcohol Dehydrogenase Gene under Heavy Metal Stress (중금속 노출에 따른 리파리 깔다구에서의 ADH 유전자의 발현 및 특성)

  • Park, Ki-Yun;Kwak, Inn-Sil
    • Environmental Analysis Health and Toxicology
    • /
    • v.24 no.2
    • /
    • pp.107-117
    • /
    • 2009
  • Metal pollution of aquatic ecosystems is a problem of economic and health importance. Information regarding molecular responses to metal exposure is sorely needed in order to identify potential biomarkers. To determine the effects of heavy metals on chironomids, the full-length cDNA of alcohol dehydrogenase (ADH3) from Chironomus riparius was determined through molecular cloning and rapid amplification of cDNA ends (RACE). The expression of ADH3 was analyzed under various cadmium and copper concentrations. A comparative and phylogenetic study among different orders of insects and vertebrates was carried out through analysis of sequence databases. The complete cDNA sequence of the ADH3 gene was 1134 bp in length. The sequence of C. riparius ADH3 shows a low degree of amino acid identity (around 70%) with homologous sequences in other insects. After exposure of C. riparius to various concentrations of copper, ADH3 gene expression significantly decreased within 1 hour. The ADH3 gene expression was also suppressed in C. riparius after cadmium exposure for 24 hour. However, the effect of cadmium on ADH3 gene expression was transient in C. riparius. The results show that the suppression of ADH3 gene by copper exposure could be used as a possible biomarker in aquatic environmental monitoring and imply differential toxicity to copper and cadmium in C. riparius larvae.

Effects of Vegetable Extracts by Solvent Separation on Alcohol Dehydrogenase Activity from Saccharomyces cerevisiae (채소의 용매분획 추출물들이 Saccharomyces cerevisiae의 alcohol dehydrogenase 활성에 미치는 영향)

  • Kang, Bae-Kwang;Jung, Soon-Teck;Kim, Seon-Jae
    • Korean Journal of Food Science and Technology
    • /
    • v.34 no.2
    • /
    • pp.244-248
    • /
    • 2002
  • The effects of extracts from bean sprout (Glycine max), dropwort (Oenathe javanica) and radish (Raphanus sativus Var. hortensis for. acanthiformis) by solvent separation on alcohol dehydrogenase (ADH) activity in vitro were investigated. The extracts were obtained from alcohol extracts of bean sprout, dropwort and radish, followed by solvent separation. Aqueous fractions facilitated much higher ADH activity than organic fractions. The facilitating rates of bean sprout, dropwort and radish in aqueous fractions were 125.75%, 104.94% and 87.63%, respectively. Basic fractions showed the highest facilitating rate with about 40%. Also other fractions showed below 20% facilitating rate and didn't show great difference from organic fractions. Phenolic fractions didn't show great effect on ADH activity.

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

  • 남석우;박승희;윤성필;서동완;남태균;홍성렬;이향우
    • Biomolecules & Therapeutics
    • /
    • v.3 no.2
    • /
    • pp.171-175
    • /
    • 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.

  • PDF

The Effect of Ginseng Saponin on Yeast Alcohol Dehydrogenase (인삼 사포닌이 효모 Alcohol Dehydrogenase에 미치는 영향)

  • 김재원;주충노
    • Journal of Ginseng Research
    • /
    • v.10 no.2
    • /
    • pp.209-217
    • /
    • 1986
  • Yeast alcohol dehydrogenates and ginseng saponin interaction has been investigated to understand the non-specific enzyme stimulating effect of the saponin of Panax ginseng C.A. Meyer. It was confirmed that several amphiphiles such as sodium dodecyl sulfate(SDS), Triton X-100, sodium taurodeoxycholate (Na-TDC) as well as ginseng saponin mixture and purified ginseng glycosides lowered Km values of yeast alcohol dehydrogenase (ADH) for ethanol and NAD in the presence of the above amphiphiles suggesting that the surface activity of the amphiphiles might play a significant role in the ADH catalyzed reactions. Conformational change of yeast alcohol dehydrogenase in the presence of the above amphiphiles at their optimal concentration for the maximum activity was studied. Circular dichroism (C.D) spectrum of yeast ADH showed that the conformational change of the enzyme occurred in the presence of above amphiphiles. Fluorescence data also showed that the hydrophobic area increased in the presence of above amphiphiles. Examination of the interaction between ADH and ginseng saponin using radioactive saponin showed that there might be a very weak interaction between them. From the above results, it was concluded that the non-specific enzyme stimulating effect of the saponin might be due to the change of polarity of the enzyme solution in the presence of the saponin.

  • PDF

Studies on Hepatic Microsomal Alcohol Dehydrogenase(ADH) and Aldehyde Dehydrogenase(ALDH) Activities in Rats Treated with Trichloroethylene (Trichloroethylene 처리한 흰쥐의 간 미크로좀 Alcohol dehydrogenase와 Aldehyde dehydrogenase 활성도에 관한 연구)

  • Kim, Ki-Woong;Kang, Seong Kyu;Yang, Jeong Sun;Park, In-Jeong;Moon, Young-Hahn
    • Journal of Korean Society of Occupational and Environmental Hygiene
    • /
    • v.4 no.2
    • /
    • pp.148-156
    • /
    • 1994
  • Chloral hydrate(CH), an intermediate metabolite of trichloroethylene(TRI) is reduced to trichloroethanol(TCE-OH), and is oxidized to trichloroacetic acid(TCA) by the nicotinamide adenine dinucleotide(NAD)-dependent enzymes such as alcohol dehydrogenase(ADH) and aldehyde dehydrogenase(ALDH) in liver. This study was performed to find out the change of activity of ADH and ALDH with increasing amount of TRI. Intraperitoneal injection of TRI were done to the male Sprague Dawely rats(mean body weight, $170{\pm}10g$) in com oil at the dosage of 150, 300, 600 mg/kg for 2 days. The results of experiments are following : 1. The contents of xenobiotic metabolic enzymes in liver are tended to be decreased with increasing amount of, but not significantlly (p>0.05). 2. Activity of ADH in microsome is decreased(p<0.05), and activity of ALDH is increased with amount of TRI(P<0.05). 3. Total trichloro-compounds(TTC) concentration in urine are increased with amount of TRI, but the ratio of between the TCE-OH and the TCA were not shown any critical change. These results suggests that the ALDH in microsome may be related to metabolism of TRI, but ADH was nothing less than the effected to metabolism of TRI.

  • PDF

Effect of Puffer Fish Extract on the Hepatic Alcohol Metabolizing Enzyme System in Alcohol-Treated Rat (Alcohol 섭취 쥐에서 Alchol 대사효소계에 미치는 복어추출물의 효과)

  • 김동훈;김동수;최종원
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.23 no.2
    • /
    • pp.181-186
    • /
    • 1994
  • The present study was undertaken to clarify the effect of Puffer fish skin extract (PF) on the hepatic alcohol metabolism in rats. It was observed that alcohol concentration in blood had been markedly decreased by the pretreatment of PF for two weeks. Activities of alcohol dehydrogenase (ADH) and microsomal ethanol-oxidizing system (MEOS) were significantly incrased (more than 20% of control) by pretreatment of PF for two weeks and acute alcohol intoxication (5 g/kg) on final day. When rats were fed with subacute toxic state by alcohol (25v/v % , once a day for six weeks), activities of ADH and MEOS were significantly increased by additional treatments of PF for final two weeks. But the catalase activity was not affected by any of both case. And also activities of ADH and MEOS in vitro were not changed . These results suggest that PF treatemnt prompted the recovery from alcohol intoxication.

  • PDF

Effect of Fermented Sea Tangle on the Alcohol Dehydrogenase and Acetaldehyde Dehydrogenase in Saccharomyces cerevisiae

  • Cha, Jae-Young;Jeong, Jae-Jun;Yang, Hyun-Ju;Lee, Bae-Jin;Cho, Young-Su
    • Journal of Microbiology and Biotechnology
    • /
    • v.21 no.8
    • /
    • pp.791-795
    • /
    • 2011
  • Sea tangle, a kind of brown seaweed, was fermented with Lactobacillus brevis BJ-20. The gamma-aminobutyric acid (GABA) content in fermented sea tangle (FST) was 5.56% (w/w) and GABA in total free amino acid of FST was 49.5%. The effect of FST on the enzyme activities and mRNA protein expression of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) involved in alcohol metabolism in Saccharomyces cerevisiae was investigated. Yeast was cultured in YPD medium supplemented with different concentrations of FST powder [0, 0.4, 0.8, and 1.0% (w/v)] for 18 h. FST had no cytotoxic effect on the yeast growth. The highest activities and protein expressions of ADH and ALDH from the cell-free extracts of S. cerevisiae were evident with the 0.4% and 0.8% (w/v) FST-supplemented concentrations, respectively. The highest concentrations of GABA as well as minerals (Zn, Ca, and Mg) were found in the cell-free extracts of S. cerevisiae cultured in medium supplemented with 0.4% (w/v) FST. The levels of GABA, Zn, Ca, and Mg in S. cerevisiae were strongly correlated with the enzyme activities of ADH and ALDH in yeast. These results indicate that FST can enhance the enzyme activities and protein expression of ADH and ALDH in S. cerevisiae.

Effect of Perilla(Perilla frutescens Britton) Extract on Serum Ethanol Level and Hepatic Alcohol Dehydrogenase Activity (소엽(蘇葉)의 추출물이 혈장알콜농도와 간의 알콜대사효소에 미치는 영향)

  • Moon, Hyung-In;Zee, Ok-Pyo;Shin, Kuk-Hyun
    • Korean Journal of Medicinal Crop Science
    • /
    • v.6 no.2
    • /
    • pp.126-130
    • /
    • 1998
  • Effects of organic solvent fractions from perilla 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 increase ethanol concentration in the blood and inhibit ADH activity.

  • PDF

Effects of Compounds Isolated from Ainsliaea acerifolia on the Hepatic Alcohol Dehydrogenase Activity (단풍취로부터 분리한 Apigenin $7-O-{\beta}-D-glucoside$가 알콜대사효소에 미치는 영향)

  • Zee, Ok-Pyo;Shin, Mal-Shick;Moon, Hyung-In
    • Applied Biological Chemistry
    • /
    • v.42 no.2
    • /
    • pp.162-165
    • /
    • 1999
  • Effects of compounds isolated from Ainsliaea acerifolia on alcohol metabolism in rats were examined and the results were as follows: Apigenin $7-O-{\beta}-D-glucoside$, 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.

  • PDF

Purification and characterization of alcohol dehydrogenase encoded by Zymomonas mobilis gene in Escherichia coli

  • 신병식;윤기홍;박무영
    • Proceedings of the Korean Society for Applied Microbiology Conference
    • /
    • 1986.12a
    • /
    • pp.521.3-522
    • /
    • 1986
  • A gene encoding alcohol dehydrogenase (ADH) in Zymomonas mobilis was cloned into E. coli JM 83 with plasmid pUC 9. The ADH produced by the E. coli transformant was purified bysonication, (NH$^4$)2SO4 fractionation, Affi-Gel blue and hydroxylapatite chromatography. The ADH produced by Z. mobilis was also purified by the same procedures. The two enzyme preparations were characterized and compared. It was found that the E. coli ADH was identical to one of two ADH isozymes of Z. mobilis. Analytical gel filtrations led to the conclusion that the molecule of E. coli ADH was composedv of four subunits having molecular weight of 40,000 (+1,000) dalton each The effect of metal ions on ADH activity and optimum pH were investigated.

  • PDF