• 제목/요약/키워드: S-transferase

검색결과 1,041건 처리시간 0.028초

창이자 및 꿀풀하고초에 의한 NAD(P)H:quinone reductase와 glutathione S-transferase의 유도 (Induction of NAD(P)H:quinone reductase and glutathione S-transferase by Xanthii Fructus and Prunellae Spica Extracts)

  • 손윤희;이기택;박신화;조경희;임종국;남경수
    • 생약학회지
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    • 제32권4호통권127호
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    • pp.269-273
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    • 2001
  • Ethanol extracts from Xanthii Fructus (XFE) and Prunellae Spica (PSE) were investigated for the effects on the induction of cancer chemoprevention-associated enzymes. The following effects were measured: (a) induction of quinone reductase (QR) (b) induction of glutathione S-transferase (GST) (c) reduced glutathione (GSH) level. XFE and PSE were potent inducers of quinone reductase activity in Hepa1c1c7 murine hepatoma cells. Glutathione levels were increased with XFE and PSE. In addition, glutathione S-transferase activity was increased with XFE. However, GST activity was not increased with PSE. These results suggest that XFE and PSE have chemopreventive potentials by inducing quinone reductase and increasing GSH levels.

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The GSTP1 Ile105Val Polymorphism is not Associated with Susceptibility to Colorectal Cancer

  • Khabaz, Mohamad Nidal
    • Asian Pacific Journal of Cancer Prevention
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    • 제13권6호
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    • pp.2949-2953
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    • 2012
  • The glutathione S transferase (GST) family is a major part of cellular defense mechanisms against endogenous and exogenous substances, many of which have carcinogenic potential. Alteration in the expression level or structure of the glutathione-S-transferase (GST) enzymes may lead to inadequate detoxification of potential carcinogens and consequently contribute to cancer development. A member of the glutathione-S-transferase (GST) family, GSTP1, is an attractive candidate for involvement in susceptibility to carcinogen-associated colorectal cancer. An $Ag{\rightarrow}G$ transition in exon 5 resulting in an Ile105Val amino acid substitution has been identified which alters catalytic efficiency. The present study investigated the possible impact of Ile105Val GSTP1 polymorphism on susceptibility to colorectal cancer. in Jordan We examined 90 tissue samples previously diagnosed with colorectal carcinoma, and 56 non-cancerous colon tissues. DNA was extracted from paraffin embedded tissues and the status of the GSTP1 polymorphism was determined using a polymerase chain reaction restriction fragment length polymorphism (RFLP) method. No statistically significant differences were found between colorectal cancer cases and controls for the GSTP1 Ile/Ile, Ile/Val and Val/Val genotypes. The glutathione S-transferase polymorphism was not associated with risk in colorectal cancer cases in Jordan stratified by age, sex, site, grade or tumor stage. In conclusion, the GSTP1 Ile105Val polymorphism is unlikely to affect the risk of colorectal cancer.

양파 추출물에서의 글루타티온 전달효소 활성 저해제에 관한 연구 (A Study of Glutathione S-transferase Inhibitors obtained from Allium cepa var. cepa Extract)

  • 이광수;박경숙
    • 한국식품영양학회지
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    • 제26권4호
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    • pp.725-730
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    • 2013
  • In this study, an ethanol extract being obtained from Allium cepa var. cepa examins the inhibitory effects on the glutathione S-transferase and the separation had been done by silica-gel column chromatography using various eluents, such as ethyl acetate, methanol, and 50% methanol. A volume of column fraction was 50ml and evaporation has been performde by the rotary evaporator under reduced pressure. Each fraction is being examined by thin layer chromatography and the UV spectrum at 365 nm was used to investigate separation patterns of spots on thin layer chromatography. When the eluent was changed, the spot patterns showed another different pattern on thin layer chromatography, so on. Fractions showing similar pattern are combined and eventually, three fractions are obtained. Each fraction is testified to examine the inhibition effects on glutathione S-transferase. All of these showed inhibition effects on glutathione S-transferase. The GC-MS shows that each fraction contains more than 2 compounds.

흰쥐에 있어서 Bromobenzene전처치가 간조직 중 Glutathione 및 Glutathione S-transferase활성에 미치는 영향 (Effect of Bromobenzene Pretreatment on the Hepatic Glutathione Content and Glutathione S-transferase Activity in Bromobenzene Treated Rats)

  • 신중규
    • 한국환경보건학회지
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    • 제23권2호
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    • pp.83-88
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    • 1997
  • To evaluate the effect of bromobenzene pretreatment on the bromobenzene metabolism, the animal group was induced the stage of slight liver damage with 7 times bromobenzene injection every two days (400 mg/kg body wt. i.p.). In the present experimental animal model, the single dose of bromobenzene(400 mg/kg body wt. i.p.) was injected to the bromobenzene-pretreated rats and the hepatic aniline hydroxylase(AH) activity, glutathione(GSH) content and glutathione S-transferase (GST) activity were determined at the intervals of 2, 4, 8, 24 hours throughout 24 hr. The activities of hepatic AH and GST were generally higher in bromobenzene-pretreated rats than those in normal group throughout the whole course of experiment. Furthermore, the decreasing rate of hepatic GSH content was also higher in bromobenzene pretreated rats than in normal rats. Moreover, the value of V$_{max}$ in hepatic GST was higher in bromobenzene pretreated rats than that in the normal rats. In conclusion, these results indicate that the pretreatment of bromobenzene may rather enhance the bromobenzene metabolism.

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

  • 최유미;김길하
    • 농약과학회지
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    • 제8권1호
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    • pp.16-21
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    • 2004
  • 본 연구는 6종 나방류(멸강나방, 배추좀나방, 목화바둑명나방, 파밤나방, 담배나방, 담배거세미나방) 대한 유충영기별 thiodicarb의 살충활성을 조사하였으며, 살충효과 구명을 위하여 효소활성(esterase, acetylcholinesterase, glutathione S-transferase)등을 검토하였다. 이 약제는 6종의 나방류 어린유충에 대해서 높은 살충효과를 나타내었으나, 노숙유충에 대한 살충효과는 상대적으로 낮았고, 발현속도는 느렸다. 담배거세미나방을 대상으로 한 효소활성저해 실험에서 acetylcholinesterase와 glutathione S-transferase 활성을 저해하였으나, esterase 활성을 저해하지는 않았다.

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 and Biomaterials
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    • 제9권1호
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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.

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

  • 이은희;조재용;차배천
    • 생약학회지
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    • 제35권3호통권138호
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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.

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

  • 유용만;홍순성;김성문;허장현
    • 농약과학회지
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    • 제7권1호
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    • pp.38-44
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    • 2003
  • 본 연구는 다양한 계열의 농약을 대상으로 체내에서 농약을 무독화하는 효소로 알려진 glutathione-S-transferase(GST) 와 esterases 에 대한 저해정도를 조사하고, 이 중 저해력이 높은 약제를 선발하여 무독화 효소에 의하여 분해되는 것으로 보고된 약제와 혼합 처리하였을 때 나타나는 약효의 변화를 조사하고자 수행하였다. 무독화효소를 저해하는 농약을 선발하기 위하여 34종의 살충제와 31종의 살균제를 대상으로 glutathione-S-transferase와 esterases 에 대한 저해력을 측정한 결과, thiodicarb $(I_{50}:1.87{\times}10^{-4}M)$, thiocyclarn $(I_{50}:7.40{\times}10^{-4}M)$, dithianon $(I_{50}:7.55{\times}10^{-5}M)$, tolylfluanide $(I_{50}:8.66{\times}10^{-5}M)$은 glutathione-S-transferase의 활성을 강게 저해하였고, dichlorvos $(I_{50}:8.95{\times}10^{-8}M)$, pirimicarb $(I_{50}:2.74{\times}10^{-6}M)$, pyrazophos $(I_{50}:3.31{\times}10^{-5}M)$, benomyl $(I_{50}:4.96{\times}10^{-5}M)$은 esterases의 활성을 강하게 저해하였다. Glutathione-S-transferase를 저해하였던 thiodicarb, thiocyclarn, dithianon, tolylfluanide와 glutathione-S-transferase 에 의해 대사되는 것으로 알려진 aeephate를 혼합 (1:1)하여 배추좀나방 (Plutella xylostella L.) 에 처리하고 약효를 관찰한 결과, 각각의 단제를 처리하였을 때보다 약효가 상승되었다. 특히 dithianon과 thiocyclam을 acephate 와 혼합시 각각 7배와 4배 약효가 상승하였다. 그리고 esterase를 저해한 약제인 dichlorvos, pirimicarb, pyrazophos, benomyl 을 esterase 에 의해 대사되는 것으로 알려진 phenthoate 와 혼합하였을 경우에도 단제 처리시의 약효보다는 혼합처리시의 약효가 높았다. Phenthoate와 dichlorvos 혼합시 18배, phenthoate 와 benomyl 혼합처리시 12배의 약효상승효과가 나타났다. 본 연구의 결과들은 무독화과정 효소에 의해 무독화되는 약제를 무독화효소 저해제와 혼합처리시 약효상승이 유발된다는 것을 나타내는데, 이러한 결과들은 향후 혼합제 개발에 유용하게 사용될 수 있을 것이라 생각된다.

제초제 검출 키트 개발을 위한 식물 해독효소 고정화 연구 (Study on the immobilization of plant glutathione S-transferase for development of herbicide detection kit)

  • 조현영;이진주;공광훈
    • 분석과학
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    • 제23권2호
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    • pp.172-178
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    • 2010
  • Glutathione S-transferase는 식물의 해독작용에 중추적인 역할을 하는 화학 효소이다. 본 연구에서는 제초제 검출 키트 개발에 응용을 위하여 식물 해독작용에 중추적인 역할을 하는 glutathione Stransferase의 고정화 방법을 연구하였다. Chloroacetanilide계 제초제에 높은 효소 활성을 보이는 벼 유래 OsGSTF3에 공유결합을 통한 polystyrene-alkylamine 비드와 리간드결합을 통한 agarose-aminoalkyl 비드,포괄법을 통한 Na-alginate 비드를 이용하여 고정화를 실시하였다. 정제된 OsGSTF3 10 mg을 사용하여 고정화 하였을 때 0.62 mg/g 비드로 polystyrene-alkylamine에 가장 효율적으로 고정화 되었다. 고정화 된 OsGSTF3의 효소 활성은 야생형의 30%를 나타내었으며, 재사용에 의한 효소활성 측정시 3회 까지 처음 활성의 80% 이상을 유지하였다.

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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    • 제31권1호
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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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