• Title/Summary/Keyword: Dehydrogenase

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

  • 김석기;이영철;서광기;최혜선
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.30 no.5
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    • pp.954-958
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    • 2001
  • Perismmon has been consumed for long times in Korea and used as a drug for a long time in Korea, It was known to help alcohol intoxication. Ingested alcohol is metabilized by alcohol dehydrogenease and acetaldehyde dehydrogenase in liver. Alcohol dehydrogenease activator and acetaldehyde dehydrogenase activator(ALDHA) was detercted in persimmon. The oncentration of ALDHA was determined and compared in different havesting time, species, and available processed foods. The level of ALDHA was highest in persimmon (Fuyu) harvested in November. Lower ALDHA activities were found in its processed foods. Persimmon and its processed foods are expected to be effective in decreasing the concentration of alcohol and acetaldehyde after alcohol intake.

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Inhibitory effect of cinnamon (Cinnamomum cassia Presl) extract and cinnamaldehyde on alcohol dehydrogenase (계피(Cinnamomum cassia Presl) 추출물과 cinnamaldehyde의 alcohol dehydrogenase 저해 효과)

  • Do, Jaeho;In, Man-Jin;Kim, Dong Chung
    • Journal of Applied Biological Chemistry
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    • v.65 no.3
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    • pp.183-187
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    • 2022
  • The hot water extract from cinnamon (Cinnamomum cassia Presl) inhibited the activity of alcohol dehydrogenase (ADH) with IC50 value of 45.6 ㎍/mL. The ADH inhibitory components in cinnamon extract were relatively stable to acid and heat, but were found to be volatile. The optimum temperature and time for extracting the ADH inhibitory components from cinnamon were 80 ℃ and 2 h, respectively. Among the essential oils of cinnamon, cinnamaldehyde was the main substance for ADH inhibition. Cinnamaldehyde is considered a competitive inhibitor of ethanol to ADH. Therefore, the cinnamon extract and cinnamaldehyde showed the potential to be used as natural materials for relieving symptoms of a hangover.

Characterization of the 5-Flanking region upstream from the structural gene for Zymononas mobilis alcohol dehydrogenase

  • Yoon, Ki-Hong;Park, Seung-Hwan;Jung, Kyung-Hwa;Pack, M. Y.
    • Journal of Microbiology
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    • v.33 no.2
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    • pp.126-127
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    • 1995
  • A Zymomonas mobilis DNA fragment consisting of 207 nucleotides, which corresponded to the 5'-flanking region of an adhB gene encoding alcohol dehydrogenase II, was fused to the structural gene coding for a Bacillus endo-.betha.--1, 4-glucanase. The Z. mobilis DNA framgment waw identified to promote 50-fold increase in the expression of endo-.betha.1. 4 glucanase gene in Escherichia coli.

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Hansenula sp. MS-364의 생육과 Formate Dehydrogenase의 활성

  • 유병욱;권태종
    • Microbiology and Biotechnology Letters
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    • v.25 no.4
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    • pp.403-407
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    • 1997
  • Medium components for maximum activity of NAD$^{+}$-dependent formate dehydrogenase (EC 1.2.1.2; FDH) were optimized with a methanol-assimilating yeast Hansenula sp. MS-364, preserved by our laboratory. The maximum activity of the enzyme was obtained when the strain was cultivated at 30$circ$C for 24 hours in a medium containing methanol 3%(v/v), yeast extract 0.8%(w/v), K$_{2}$HPO$_{4}$, 0.1%(w/v), KH$_{2}$PO$_{4}$ 0.1%(W/V), MgSO$_{4}$, 7H$_{2}$O 0.05%(w/v), and the pH of the culture broth was adjusted at 5.0.

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Synthesis of $\beta$-Hydroxy-Propenamide Derivatives and the Inhibition of Human Dihydroorotate Dehydrogenase

  • Kim, Taek-Hyeon;Na, Hye-Sun;Loffler, Monika
    • Archives of Pharmacal Research
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    • v.26 no.3
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    • pp.197-201
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    • 2003
  • Novel $\beta$-hydroxy propenamides as analogues of the active metabolite of leflunomide (A 771726) were synthesized and evaluated for their inhibitory activity on dihydroorotate dehydrogenase (DHODH) in an investigation into their immunosuppressive activity. Compounds 2a, 3a, and 3h were approximately 4-40 times more potent than leflunomide in their activity while they were-less active than A 771726.

Characterization of 2-hydroxymuconic semialdehyde dehydrogenase from Burkholderia cepacia G4

  • A. Matta Reddy;Min, Kyung-Rak;Kim, Young-Soo
    • Proceedings of the PSK Conference
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    • 2003.04a
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    • pp.218.2-219
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    • 2003
  • 2-Hydroxymuconic semialdehyde dehydrogenase catalyzes the conversion of 2-hydroxymuconic semialdehyde (HMS) to an enol form of 4-oxalocrotonate which is a step in the catechol-meta cleavage pathway. A tomC gene encoding 2-HMS dehydrogenase of Burkholderia cepacia G4, a soil bacterium that can grow on toluene, cresol, phenol or tricholoro ethylene, is identified in between catechol 2,3-dioxygenase gene and HMS hydrolase gene, its sequence is analysed and the enzyme is characterised. (omitted)

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Assay of Glucose-6-phosphate Dehydrogenase in E. coli Cells Ruptured by Phage Ghost (Phage Ghost로 破裂시킨 E. coli 에서 Glucose-6-phosphate Dehydrogenase의 活性度 測定)

  • Yun, Se-Joong
    • Journal of the Korean Chemical Society
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    • v.12 no.4
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    • pp.142-145
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    • 1968
  • The relative activity of glucose-6-phosphate dehydrogenase in E. coli was measured at 340 $m\mu$ with a spectrophotometer. The synchronized E. coli cells in exponential phase were treated with Phage($T_2$) ghost, and used as a enzyme solution directly. This assay method supposed to be useful for the continuous determination of enzyme activity in E. coli.

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Separation of Dehydrogenase Isozymes by Cellulose Acetate Electrophoresis (Cellulose Acetate 전기영동에 의한 수소이탈효소 Isozyme의 분리)

  • 박상윤;조동현
    • The Korean Journal of Zoology
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    • v.15 no.3
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    • pp.101-104
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    • 1972
  • A simple and economical method for separation of lactate and malate dehydrogenase isozymes is described in detail. The method is based on cellulose acetate strip electrophoretic separation of the isozymes, tetrazolium reduction to purple formazan. Resolution is as good as in the experiment using expensive equipments.

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The Activity of Succinic Dehydrogenase During the Metamorphosis on the Pine Moth, Dendrolimus spectabilis BUTLER (송충의 변태에 따른 Succinic Dehydrogenase 의 활성도)

  • 김창환;류종명
    • The Korean Journal of Zoology
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    • v.9 no.2
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    • pp.7-9
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    • 1966
  • 송충(Dendrolimus spectabilis)의 변태에 따른 succinic dehydrogenase 의 활성도를 Thunberg 관법을 이용하여 측정하였다. 일반적으로 생성도의 변동은 기관발생과 밀접한 관계를 가지고있으며 각 기관에 있어서의 활성도는 아래와같다. 1. Gut는 여러 기관중 제일 높은 활성도를 보여주며 fat body 와 더불어 U자 모양 curve의 활성도를 나타내고 있다. 2. Brain 과 testis 는 상승의 활성도를 보여주었다. 3. Body wall 과 verve cord의 활성도는 불규칙적이었다.

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