• 제목/요약/키워드: S-transferase

검색결과 1,041건 처리시간 0.029초

Characterization of Uridine-Diphosphate Dependent Flavonoid Glucosyltransferase from Oryza sativa

  • Hong, Byoung-Seok;Kim, Jeong-Ho;Kim, Na-Yeon;Kim, Bong-Gyu;Chong, You-Hoon;Ahn, Joong-Hoon
    • BMB Reports
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    • 제40권6호
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    • pp.870-874
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    • 2007
  • We cloned a uridine-diphosphate dependent glycosyl-transferase RUGT-10 from Oryza sativa. The recombinant enzyme was expressed by glutathione-S transferase gene fusion system in Escherichia coli. RUGT10 showed different regioselectivity depending on the structures of substrates (e.g. flavanone, flavonol, and flavone). Apparently, flavanone such as naringenin and eriodictyol gave one 7-O-glucoside while flavone and flavonol gave more than two products with preferential glucosylation position of hydroxyl group at C-3 position.

Inhibitory activity of diarylheptanoids on farnesyl protein transferase

  • Kang, Hyun-Mi;Jeon, Sun-Bok;Son, Kwang-Hee;Yang, Deok-Cho;Han, Dong-Cho;Kwon, Byoung-Mog
    • 대한약학회:학술대회논문집
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    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.1
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    • pp.265.2-265.2
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    • 2003
  • Diarylheptanoids [curcumin (1), demethoxycurcumin (2), bisdemethoxycurcumin (3), bisdimethoxymethylcurcumin (4), and 1,2-dihydrobis(de-O-methyl)curcumin (5)] were isolated from the methanolic extract of Curcuma longa L. and A new cyclic diarylheptanoiid (6) and a known compound 7 were isolated from fruits of Alnus japonica S. Diarylheptanoids (1-3) inhibited farnesyl protein transferase (FTPase) with an IC50 of 29-50 $\mu\textrm{m}$. (omitted)

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KIF5s와 직접 결합하는 액틴 결합 운동단백질 Myo9s의 규명 (Direct Interaction of KIF5s and Actin-Based Transport Motor, Myo9s)

  • 석대현
    • 생명과학회지
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    • 제21권8호
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    • pp.1076-1082
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    • 2011
  • 미세소관(microtubule) 위를 이동하는 키네신은 분비소포를 이동시키는 운동단백질이다. KIF5s (KIF5A, KIF5B and KIF5C)는 세포막으로 싸인 각종 세포 내 소기관과 결합하여 미세소관을 따라 목적지까지 이동시킨다는 결과는 알려져 있지만, 어떻게 상대의 cargo를 인식하는지는 밝혀지지 않았다. 본 연구는 KIF5B의 결합 단백질을 동정하기 위하여 효모 two-hybrid system을 사용하여 KIF5B와 특이적으로 결합하는 Myo9b을 확인하였다. Myo9b는 액틴위를 이동하는 운동단백질로 다른 KIF5s들과도 결합함을 효모 two-hybrid assay로 확인하였다. 또한 Myo9s의 GTPase 활성화 단백질(GAP) 영역은 KIF5B와 결합하는데 필수영역임을 확인하였고, 이러한 단백질간의 결합은 Glutathione S-transferase (GST) pull-down assay를 통하여서도 확인하였다. 생쥐의 뇌 파쇄액에 KIF5B들의 항체로 면역침강을 행하여 Myo9s 단백질을 확인한 결과, KIF5s는 Myo9s 단백질과 특이적으로 함께 침강하였다. 이러한 결과들은 kinesin-I는 액틴 결합 운동단백질과 직접 결합함을 보여준다.

Hepatoprotective activity of terpenoids and terpenoid fractions of Scoparia dulcis L

  • Krishnamurthy, Praveen Thaggikuppe;Bajaj, Jitendra;Sharma, Abhishek;Manimaran, Sellappan;Ravanappa, Prashantha Kumar Bommenahalli;Pottekad, Vijayan
    • Advances in Traditional Medicine
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    • 제10권4호
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    • pp.263-270
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    • 2010
  • Scoparia dulcis L. is widely used in the traditional system of medicine for treating liver ailments. In the present study the terpenoids and terpenoid fractions isolated from 1:1:1 petroleum ether, diethyl ether and methanol (PDM) extract of Scoparia dulcis L. were tested for their in vitro 1, 1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity. Selected samples from the assay were further tested for their in vitro hepatoprotective activity against $CCl_4$ induced hepatotoxicity in freshly isolated rat hepatocytes. In the in vitro antioxidant study, fractions 7, 11, 13, 14, and 15 and PDM extract show the DPPH radical scavenging activity. The phytochemical screening of all these fractions show the presence of terpenoids. In the in vitro hepatoprotective study all these fractions and the PDM extract significantly prevent the $CCl_4$ induced changes in the aspartate aspartate amino transferase, alanine amino transferase and alkaline phosphatase levels (p < 0.05). The above results are comparable with the standard, silymarin. The results of the study indicate that, the PDM extract of Scoparia dulcis L. possesses potential hepatoprotective activity and this may be attributed to its free radical scavenging potential, which in turn may be attributed to the presence of terpenoids.