• Title, Summary, Keyword: glutathione S-transferase

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Insecticidal activity of thiodicarb on lepidopterous pests (나방류에 대한 thiodicarb의 살충활성)

  • Choi, Yu-Mi;Kim, Gil-Hah
    • The Korean Journal of Pesticide Science
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    • v.8 no.1
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    • pp.16-21
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    • 2004
  • A series of experiments was conducted to determine the toxicities of thiodicarb on the six lepidopterous pests (Pseudaletia separata, Plutella xylostella, Palpita indica, Spodoptera exigua, Helicoverpa assulta, Spodoptera litura) and to elucidate factors insecticidal effects mechanism of thiodicarb. Thiodicarb was very effective against six lepidopterous young larvae, but less effective to the old larvae and it acted slowly. Thiodicarb inhibited acetylcholinesterase and glutathione S-transferase activities, but not inhibit esterase activity.

Glutathione S-transferase Activity and Hyaluronidase Inhibitory Effect of Medicinal Plants (생약의 Glutathione S-transferase 활성과 Hyaluronidase 저해효과)

  • Lee, Eun-Hee;Cho, Jae-Yong;Cha, Bae-Cheon
    • Korean Journal of Pharmacognosy
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    • v.35 no.3
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    • pp.184-188
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    • 2004
  • This study was carried out to evaluate glutathione S-transferase (GST) activity and hyaluronidase inhibitory effect of medicinal plants. The EtOH extracts of 20 species plants were tested. As the result, Acorus gramineus and Pueraria lobata exhibited GST activity. On the continuous experiment, the n-BuOH fraction of Acorus gramineus and the $H_2O$ fraction of Pueraria lobata showed the elevation of GST activity. On the experiment of hyaluronidase inhibitory effect, Acorus gramineus exhibited a potent inhibitory activity. These results suggest that the extract of Acorus gramineus can be applicable for the development of a new anti-inflammatory agent.

Molecular Cloning and mRNA Expression a Glutathione S-Transferase cDNA from the Spider, Araneus ventricosus

  • Shin, Geun Ho;Kim, Hyung Suk;Kwon, Dong Wook;Lee, Jin Young;Byeon, Gyeong Min;Sohn, Hung Dae;Jin, Byung Rae
    • International Journal of Industrial Entomology
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    • v.9 no.1
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    • pp.65-71
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    • 2004
  • A fat body-specific glutathione S-transferase cDMA was cloned from the spider, Araneus ventricosus. The cDNA encoding A. ventricosus glutathione S-transferase (AvGST) is 645 base pairs long with an open reading frame of 215 amino acid residues with a calculated molecular weight of approximately 24 kDa. Northern blot analysis showed the tissue-specifically expression of AvGST in the A. ventricosus fat body.

Effect of Polysaccharide from Trichosanthes kirilowii on Antidiabetic Activity and Glutathione Metabolism in Hyperglycemic Rats (괄루근으로부터 추출한 다당류의 항당뇨활성 및 당뇨성 쥐의 글루타치온대사에 미치는 영향)

  • 정연봉;이종철
    • YAKHAK HOEJI
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    • v.39 no.5
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    • pp.528-534
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    • 1995
  • This investigation was aimed at the study of the antidiabetic activity and effect on hepatic glutathione metabolism of polysaccharide from Trichosanthes kirilowii in hyperglycemic rats with aboxan (175 mg/Kg, i.p.). As the results, the polysaccharide inhibited the increase of blood glucose, triglyceride level and lactate dehydrogenase activity, but cholesterol not changed. And it increased protein bound-SH, nonprotein bound-SH, glutathione level and inhibited the decrease of glutathione S-transferase.

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Biotransformation of the Fungicide Chlorothalonil by Bacterial Glutathione S-Transferase

  • Kim, Young-Mog;Park, Kun-Bawui;Choi, Jun-Ho;Kim, Jang-Eok;Rhee, In-Koo
    • Journal of Microbiology and Biotechnology
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    • v.14 no.5
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    • pp.938-943
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    • 2004
  • A gene responsible for the chlorothalonil-biotransformation was cloned from the chromosomal DNA of Ochrobactrum anthropi SH35B, an isolated bacterium strain from soil. We determined the nucleotide sequences and found an open reading frame for glutathione S-transferase (GST). The drug-hypersensitive Escherichia coli KAM3 cells transformed with a plasmid carrying the GST gene can grow in the presence of chlorothalonil. The GST of O. anthropi SH35B was expressed in E. coli and purified by affinity chromatography. The fungicide chlorothalonil was rapidly transformed by the purified GST in the presence of glutathione. No significant difference in the chlorothalonil-biotransformation effect was observed among the thiol compounds (cysteine, reduced glutathione, and $\beta$-mercaptoethanol). Thus, the result reported here is the first evidence on the chlorothalonil-biotransformation by conjugation with the cellular free thiol groups, especially glutathione, catalyzed by the bacterial GST.

Influence of Gami-oryungsan on bromobenzene-induced liver injury in experimental animal (Bromobenzene독성(毒性)에 의한 간기능손상(肝機能損傷)에 미치는 가미오령산의 영향(影響))

  • Kim, Jong-Dae
    • The Journal of Internal Korean Medicine
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    • v.21 no.1
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    • pp.108-115
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    • 2000
  • Objective : To investigate the hepatoprotective effects of Gami-oryungsan on the liver damage induced by bromobenzene. Method : The development of fibrosis and acute liver injury was examined by the chemical analysis of AST, AL T, ${\gamma}$-GTP . and epoxide hydrolase glutathione S-transferase glutathione peroxidase enzyme activity, lipidoperoxide levels, glutathione levels were measured and oberved. Results : The increasing levels of lipidoperoxide was decreased proportionally according to dose of extract GO. Epoxide hydrolase glutathioneS-transferase glutathione peroxidase enzyme activity highly increased in GO pre-acupunctured group compared with the group treated with only bromobenzene. The increase of serum AST, AL T, ${\gamma}$-GTP enzyme activity of mice by bromobenzene was inhibited by the administration of GO. Lipidoperoxide levels in rat's liver decreased compared to the case of bromobenzene-treated group. The levels of Glutathione decreased by bromo benzene were increased highly in GO pre-acupunctured group. Conclusion : These results suggest that GO extract recovers the damage of liver due to bromobenzene intoxication by decreasing the lipid peroxidation AST AL T ${\gamma}$-GTP enzyme activity and increasing epoxide hydrolase glutathioneS-transferase glutathione peroxidase enzyme activity, glutathione levels.

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The Study of Pretreated GE-132 on the Hepatic Glutathione S-Transferase Activity in Rat (유기게르마늄(GE-132) 이 Glutathone S-Transferase활성에 미치는 영향)

  • Kim, Seok-Hwan;Park, Eun-Sook;Jo, Tae-Hyun;Choi, Jong-Won
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.23 no.4
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    • pp.581-586
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    • 1994
  • The study was initiated elucidate the mechanism by examining the effect of GE-132 on hepatic glutathione S-transferase (GST) activity. Activity of GST increased with dose-dependent manner in hepatic cytosolic fraction of GE-132 treatment rats. Double reciprocal plotting gave Vmax value 1.4 fold increase by the treatment of GE-132(100mg/kg, p.o.for 6 weeks) compared with control group, but did not change Km value. Ethacryinc acid (85mg/kg, once a day, i.p) was injected to control rat, the GST activity decreased remarkably . However, GE-132 pretreated group, the effect caused by ethacrynic acid was markedly reduced. And activity of ${\gamma}$-glutamylcys- teine synthetase was not changed either by GE-132 treatment , but the activity of glutathione reudctase increased significantly. Decreasing properties of ethacrynic acid decreased level of hepatic glutathione , which was restored to same degree by GE -132 pretreatment . GE-132 protective effect on ethacrynic acid-induced mortality. It is concluded that the efect of GE-132 is partly mediated by increase in hepatic GST activity.

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Functional Studies of Cysteine Residues in Human Glutathione S-Transferase P1-1 by Site-Directed Mutagenesis

  • Park, Hui Jung;Lee, Gwang Su;Gong, Gwang Hun
    • Bulletin of the Korean Chemical Society
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    • v.22 no.1
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    • pp.77-83
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    • 2001
  • To gain further insight into the relationship between structure and function of glutathione S-transferase (GST), the four cysteine mutants, C14S, C47S, C101S and C169S, of human GST P1-1 were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized glutathione (GSH). The catalytic activities of the four mutant enzymes were characterized with five different substrates as well as by their binding to four different inhibitors. Cys14 seems to participate in the catalytic reaction of GST by stabilizing the conformation of the active-site loop, not in the GSH binding directly. The substitution of Cys47 with serine significantly reduces the affinity of GSH binding, although it does not prevent GSH binding. On the other hand, the substitution of Cys101 with serine appears to change the binding affinity of electrophilic substrate by inducing a conformational change of the $\alpha-helix$ D. Cys169 seems to be important for maintaining the stable conformation of the enzyme. In addition, all four cysteine residues are not needed for the steroid isomerase activity of human glutathione S-transferase P1-1.

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An Efficient System for the Expression and Purification of Yeast Geranylgeranyl Protein Transferase Type I

  • Kim, Hyun-Kyung;Kim, Young-Ah;Yang, Chul-Hak
    • BMB Reports
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    • v.31 no.1
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    • pp.77-82
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    • 1998
  • To purify the geranylgeranyl protein transferase type I (GGPT-I) efficiently, a gene expression system using the pGEX-4T-1 vector was constructed. The cal1 gene, encoding the ${\beta}$ subunit of GGPT-I, was subcloned into the pGEX-4T-1 vector and co-transformed into E. coli cells harboring the ram2 gene, the ${\alpha}$ subunit gene of GGPT-I. GGPT-I was highly expressed as a fusion protein with glutathione S-transferase (GST) in E. coli, purified to homogeneity by glutathione-agarose affinity chromatography, and the GST moiety was excised by thrombin treatment. The purified yeast GGPT-I showed a dose-dependent increase in the transferase activity, and its apparent $K_m$ value for an undecapeptide fused with GST (GST-PEP) was $0.66\;{\mu}M$ and the apparent value for geranylgeranyl pyrophosphate (GGPP) was $0.071\;{\mu}M$.

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Synergistic action of pesticide mixtures using glutathione-s-transferase- and esterase-inhibiting properties in diamondback moth (Plutella xylostella L.) (Glutathione-S-transferase와 esterase 효소 저해특성을 이용한 농약의 혼합 상승효과)

  • Yu, Yong-Man;Hong, S.S.;Kim, S.;Hur, J.H.
    • The Korean Journal of Pesticide Science
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    • v.7 no.1
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    • pp.38-44
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    • 2003
  • In vitro inhibitory activity of 34 insecticides and 31 fungicides to glutathione-S-transferase and esterases extracted from rats was determined. Of tested pesticides, the pesticides with high activity on both detoxifying enzymes were mixed with pesticides that are known to be detoxified by detoxifying enzymes. Glutathione-S-transferase was inhibited by thiodicarb $(I_{50}:1.87\times10^{-4}M)$, thiocyclam $(7.40\times10^{-4}M)$, dithianon $(7.55\times10^{-5}M)$, and tolylfluanide $(8.66\times10^{-5}M)$, while esterases by dichlorvos $(8.95\times10^{-8}M)$, pirimicarb $(2.74\times10^{-6}M)$, pyrazophos $(3.31\times10^{-5}M)$, and benomyl $(4.96\times10^{-5}M)$. After acephate known to be detoxified by glutathione-S-transferase was mixed with glutathione-S-transferase-inhibiting pesticides and phenthoate known to be detoxified by esterases was mixed with esterases-inhibiting pesticides, insecticidal activities of such mixtures were determined against diamondback moth (PlutelLa xylostella L.). Synergistic action was observed in all pesticide combinations. The highest synergistic action was obtained when phenthoate was combined with dichlorvos, showing that co-toxicity coefficients were 1512 and 1877 after 24 and 48 hours of treatment, respectively. Several other combinations of pesticides, such as phenthoate with benomyl, and acephate with dithianon, also showed synergism, showing that their co-toxicity coefficients were about 1,000 and 500, after 24 hours of treatment, respectively. Our results showed that combinations of pesticides inhibited by detoxifying enzymes and ones detoxified by detoxifying enzymes resulted in increased toxicities of pesticides, suggesting that such combinations could be used to develop pesticide mixtures with more broad spectrum and high effectiveness.