• Title, Summary, Keyword: Succinate Dehydrogenase

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Histochemical studies on effect of low concentrated carbon monoxide on the caudate nucleus in rat (저농도 일산화탄소가 흰쥐 미상핵에 미치는 영향에 관한 조직화학적 연구)

  • Kim, Jin-sang
    • Korean Journal of Veterinary Research
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    • v.29 no.4
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    • pp.425-431
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    • 1989
  • This study was undertaken to investigate the changes of enzyme activities resulted from low concentrated carbon monoxide poisoning on the caudate nucleus in rat. The activities of cytochrome oxidase, succinate dehydrogenase and lactate dehydragenase were observed histochemically, after the experimental animals were poisoned to 100ppm carbon monoxide for 8 hours every day from one day to 16 days. The materials were sliced from coronal section at the level of the optic chiasm and immediately frozen sections of $10{\mu}m$ thickness were cut on the cryostat at $-15^{\circ}C$ and incubated in the medium containing substrate for histochemical detection of cytochrome oxidase, succinate dehydrogenase and lactate dehydrogenase. The sections were mounted in glycerol gelatin and observed under light microscope. It was obtained that cytochrome oxidase activity decreased moderately and succinate dehydrogenase activity showed marked or moderate activity during entire poisoning period and lactate dehydrogenase activity showed marked or moderate activity from one to 8 days but recovered to normal condition at 16th day.

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The utilization of acetate for the growth and the respiration in Dunaliella tertiolecta.―Enzymes of the tricarboxylic acid cycle and glyoxylate pathway (Dunaliella tertiolecta에 의한 acetate의 이용 -TCA cycle과 glyoxylate pathway의 활성 조사-)

  • 권영명
    • Journal of Plant Biology
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    • v.16 no.1_2
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    • pp.6-11
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    • 1973
  • The utilization of acetate by Dunaliella tertiolecta was examined, and the detections and assays of the enzymes of the tricarboxylic acid cycle and the glyoxylate pathway were described. Acetate could not be utilized as a sole carbon source for the growth. The carboxyl carbon of acetate was incorporated more rapidly into CO2 than the methyl carbon. It was identified that malate, succinate, citrate and etc., were accumulated whne [U-14C] acetate was supplied to the cell free homogenate. The following enzyme activities were measured; acetothiokinase, isocitrate dehydrogenase, fumarase, malate dehydrogenase and aconitase. Though isocitratase, malate synthetase, succinate dehydrogenase and oxoglutarate dehydrogenase could not be detected, 14C from succinate was easily contributed to CO2 and cell component. The evidence suggested that the glyoxylate pathway was not operative and showed that the TCA cycle was the all important pathway in the oxidation of acetate to CO2 in Dunaliella.

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Development of succinate producing Cellulomonas flavigena mutants with deleted succinate dehydrogenase gene

  • Lee, Heon-Hak;Jeon, Min-Ki;Yoon, Min-Ho
    • Korean Journal of Agricultural Science
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    • v.44 no.1
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    • pp.30-39
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    • 2017
  • This study was performed to produce succinic acid from biomass by developing mutants of Cellulomonas flavigena in which the succinate dehydrogenase gene (sdh) is deleted. For development of succinate producing mutants, the upstream and downstream regions of sdh gene from C. flavigena and antibiotic resistance gene (neo, bla) were inserted into pKC1139, and the recombinant plasmids were transformed into Escherichia coli ET12567/pUZ8002 which is a donor strain for conjugation. C. flavigena was conjugated with the transformed E. coli ET12567/pUZ8002 to induce the deletion of sdh in chromosome of this bacteria by double-crossover recombination. Two mutants (C. flavigena H-1 and H-2), in which sdh gene was deleted in the chromosome, were constructed and confirmed by PCR. To estimate the production of succinic acid by the two mutants when the culture broth was fermented with biomass such as CMC, xylan, locust gum, and rapeseed straw; the culture broth was analyzed by HPLC analysis. The succinic acid in the culture broth was not detected as a fermentation products of all biomass. One of the reasons for this may be the conversion of succinic acid to fumaric acid by sdh genes (Cfla_1014 - Cfla_1017 or Cfla_1916 - Cfla_1918) which remained in the chromosomal DNA of C. flavigena H-1 and H-2. The other reason could be the conversion of succinyl-CoA to other metabolites by enzymes related to the bypass pathway of TCA cycle.

Alterations of Antioxidant Status and Mitochondrial Succinate Dehydrogenase Activity in the Liver of Wistar Strain Albino Rats Treated with by Ethanol Extracts of Annona senegalensis Pers (Annonaceae) Stem Bark

  • Adisa, Rahmat Adetutu;Kolawole, Naimat;Sulaimon, Lateef A.;Brai, Bathlomew;Ijaola, Abraham
    • Toxicological Research
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    • v.35 no.1
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    • pp.13-24
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    • 2019
  • Numerous ethnomedicinal uses have been attributed to different parts of Annona senegalensis (ASE), including its uses as food and food additives. The present study investigated toxicological and antioxidant effects of 28 days administration of ethanol extracts of ASE stem bark to Wistar strain albino rats. Acute toxicity test was done to determine lethal dose in Wistar rats while sub-acute toxicity test was conducted on rats divided into four groups (A - control, B - 50 mg/kg, C - 100 mg/kg, D - 150 mg/kg, respectively and treated for 28 days. Oxidative stress markers in liver and kidney as well as hepatic succinate dehydrogenase activity in the mitochondrial and post mitochondrial fractions (PMF) were evaluated. The $LD_{50}$ value of ASE was > 2,000 mg/kg. White blood cell counts gradually increased, but red blood cell counts and haematocrits level decreased significantly (p < 0.05) by about 50%. Liver enzymes in the serum and mitochondrial succinate dehydrogenase activity increased significantly (p < 0.05). Superoxide dismutase and catalase activities also increased in liver mitochondria and PMF while malondialdehyde (MDA) and reduced glutathione levels increased only in the PMF. Furthermore, only MDA levels increased significantly in the kidney after 28 days extract administration. Histopathological examination showed hepatic necrosis and no obvious signs of nephrotoxicity. Anona senegalensis is relatively safe, but prolonged ingestion could induce oxidative stress and impair ATP synthesis through the modulation of the activity of mitochondrial succinate dehydrogenase.

Structure-Activity Relationships of Fungicidal N-Substituted Phenyl 1,3,5- Trimethylpyrazole-4-carboxamides in the Inhibition of Succinate Dehydrogenase (SDH) Isolated from Rhizoctonia solani $K{\ddot{u}}hn$ (벼 잎집무늬 마름병균 (Rhizoctonia solani $K{\ddot{u}}hn$)에서 분리한 Succinate Dehydrogenase (SDH) 에 대한 N-치환 phenyl 1,3,5-trimethylpyrazole-4-carboxamide 유도체의 효소활성저해)

  • Kim, Yong-Whan
    • Applied Biological Chemistry
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    • v.40 no.5
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    • pp.447-450
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    • 1997
  • Eighteen N-substituted phenyl 1, 3, 5-trimethylpyrazole-4-carboxamides were synthesized to screen for their mycelial growth inhibition activity against Rhizoctonia solani $K{\ddot{u}}hn$ $(pEC_{50})$ and to measure enzymatic inhibition activity of these compounds $(pI_{50})$ against succinate dehydrogenase (SDH) isolated from Rhizoctonia solani $K{\ddot{u}}hn$ A structure-activity relationship formulated by regression analysis showed that 79% of the variance in mycelial growth inhibition activity can be explained with SDH inhibition activity and chromatographic capacity factor $(\acute{k})$ as a hydrophobic parameter related to the penetration and transport processes in the biological system.

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Effects of Local Anesthetics on Electron Transport and Generation of Superoxide Radicals in Mitochondria (국소마취제가 Mitochondria에서의 전자이동 및 Superoxide Radicals의 생성에 미치는 영향)

  • Lee, Chung-Soo;Shin, Yong-Kyoo;Lee, Kwang-Soo
    • The Korean Journal of Pharmacology
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    • v.23 no.2
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    • pp.113-121
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    • 1987
  • Local anesthetics were investigated for their effects on mitochondrial electron transport system, production of superoxide radical from submitochondrial particles and malondialdehyde production through lipid per oxidation. Local anesthetics had various effects on activities of enzymes in electron transport chain. The activities of NADH dehydrogenase, NADH oxidase and NADH-ubiquinone oxidoreductase were effectively inhibited by lidocaine, procaine and dibucaine but slightly influenced by cocaine. The activities of succinate dehydrogenase, succinate-cytochrome c oxidoreductase and succinate-ubiquinone oxidoreductase were inhibited by lidocaine and dibucaine, but the succinate oxidase activity was stimulated by local anesthetics. Both dihydroubiquinone-cytochrome c oxidoreductase and cytochrome c oxidase activities were inhibited by local anesthetics. In these reactions, the response of Complex I segment to local anesthetics was greater than other Complex segments. Local anesthetics inhibited both the superoxide production from submitochondrial particles supplemented with succinate or NADH and the enhanced production of superoxide radicals by antimycin. The malondialdehyde production by oxygen free radicals was inhibited by local anesthetics. These results suggest that the inhibition of superoxide and malondialdehyde production caused by local anesthetics may be brought by suppression of the electron transport in mitochondria at sites in or near complex I segment.

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Molecular Mechanisms of Succinate Dehydrogenase Inhibitor Resistance in Phytopathogenic Fungi

  • Sang, Hyunkyu;Lee, Hyang Burm
    • Research in Plant Disease
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    • v.26 no.1
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    • pp.1-7
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    • 2020
  • The succinate dehydrogenase inhibitor (SDHI) is a class of fungicides, which is widely and rapidly used to manage fungal pathogens in the agriculture field. Currently, fungicide resistance to SDHIs has been developed in many different plant pathogenic fungi, causing diseases on crops, fruits, vegetables, and turf. Understanding the molecular mechanisms of fungicide resistance is important for effective prevention and resistance management strategies. Two different mechanisms have currently been known in SDHI resistance. The SDHI target genes, SdhB, SdhC, and SdhD, mutation(s) confer resistance to SDHIs. In addition, overexpression of ABC transporters is involved in reduced sensitivity to SDHI fungicides. In this review, the current status of SDHI resistance mechanisms in phytopathogenic fungi is discussed.

Isolation of Inhibitor against Mouse Carcinoma Cells from Streptomyces sp. (복수세포의 Succinate Dehydrogenase 조해물질의 검색)

  • 송방호
    • Microbiology and Biotechnology Letters
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    • v.7 no.2
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    • pp.97-102
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    • 1979
  • An actinomycete, AS-568, which produced an inhibitory substance against succinate dehydrogenase of Ehrlich ascites carcinoma and Sarcoma-180 cells of mouse, was isolated. The inhibitory activity was determined by SDI (Succinate Dehydrogenase Inhibition) method. The active substance was specific against carcinoma cells compared to normal cells in mouse; liver, kidney and brain. The inhibitory ratio was about 50% after one hr treatment at 37$^{\circ}C$ in vitro. Maximal productivity of active substance was recognized by 5 days culture in glucose-asparagine. The active component in cultural liquid was stable in neutral pH range and heat treatment reasonably, add it was recovered from precipitate by ammonium sulfate or non-dialyrable fraction in cellophane membrane as showing the behavior of high molecular substance.

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Repression of Cyclohexanol Dehydrogenase in Acinetobacter calcoaceticus C10 (Acinetobacter calcoaceticus C10에서 Cyclohexanol Dehydrogenase의 생합성 억제)

  • Park, Heui Dong;Park, Jong Sung;Rhee, In Koo
    • Current Research on Agriculture and Life Sciences
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    • v.5
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    • pp.68-74
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    • 1987
  • The growth of A calcoaceticus C10 in CL medium was not increased by the addition of 0.5% E-capralactone or succinate, but increased by 0.2% adipate, xylose or even glucose which was not metabolized as a carbon source. The addition of 0.2% glucose after culture in CL medium for 6 hours increased the growth of A. colcoaceticus C10 twice as much as that in CL medium after culture for further 10 hours. Biosynthesis of cyclohexanol dehydrogenase in A. calcoaceticus C10 was not repressed by ${\varepsilon}$-caprolactone, succinate, xylose and glucose, but repressed by adipate which is endproduct of cyclohexanol metabolism. The induction of dehydrogenase by cyc1ohexanol in CL medium was not repressed completely by 0.1% adipate, but repressed almost completely by 0.2% adipate in A. calcoaceticus C10.

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