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In vitro Antioxidant Activity of Ethanolic Extract of Chlorophytum borivilianum
R. Govindarajan1,,N. Sreevidya1,,M. Vijayakumar1,,M. Thakur2,,V.K. Dixit2,,S. Mehrotra*1,,P. Pushpangadan1 한국생약학회 2005 Natural Product Sciences Vol.11 No.3
Chlorophytum borivilianum Baker (Antharicaceae) comonly referred as ‘Safed Musli’ has beenwidely used in the Indian traditional systems of medicine to treat various diseases like rheumatism apart fromaphordisiac properties. C. borivilianum was screened for the first time to determine its antioxidant activity,isolation of the sapogenins and standardization of the isolated sapogenin fraction using HPTLC. Potent antioxidantactivity of ethanolic extract was found by their ability to scavenge DPPH (84.51%), hydroxyl radical (48.95 %),feryl bi-pyridyl complex (84.53%) along with the inhibition of lipid peroxidation (67.17%) at 100g/mlconcentration. The ethanolic extract also exhibited significant inhibition of superoxide anion radical generated byplant in the traditional system especially its use as a Rasayana drug.
Identification of Inhibitors Against BAK Pore Formation using an Improved in vitro Assay System
송승수,이원규,Sreevidya Aluvila,오경준,유연규 대한화학회 2014 Bulletin of the Korean Chemical Society Vol.35 No.2
The pro-apoptotic BCL-2 family protein BID activates BAK and/or BAX, which form oligomeric pores in the mitochondrial outer membrane. This results in the release of cytochrome c into the cytoplasm, initiating the apoptotic cascade. Here, we utilized liposomes encapsulating sulfo-rhodamine at a controlled temperature to improve upon a previously reported assay system with enhanced sensitivity and specificity for measuring membrane permeabilization by BID-dependent BAK activation. BAK activation was inhibited by BCL-XL protein but not by a mutant protein with impaired anti-apoptotic activity. With the assay system, we screened a chemical library and identified several compounds including trifluoperazine, a mitochondrial apoptosisinduced channel blocker. It inhibited BAK activation by direct binding to BAK and blocking the oligomerization of BAK.
Identification of Inhibitors Against BAK Pore Formation using an Improved in vitro Assay System
Song, Seong-Soo,Lee, Won-Kyu,Aluvila, Sreevidya,Oh, Kyoung Joon,Yu, Yeon Gyu Korean Chemical Society 2014 Bulletin of the Korean Chemical Society Vol.35 No.2
The pro-apoptotic BCL-2 family protein BID activates BAK and/or BAX, which form oligomeric pores in the mitochondrial outer membrane. This results in the release of cytochrome c into the cytoplasm, initiating the apoptotic cascade. Here, we utilized liposomes encapsulating sulfo-rhodamine at a controlled temperature to improve upon a previously reported assay system with enhanced sensitivity and specificity for measuring membrane permeabilization by BID-dependent BAK activation. BAK activation was inhibited by BCL-$X_L$ protein but not by a mutant protein with impaired anti-apoptotic activity. With the assay system, we screened a chemical library and identified several compounds including trifluoperazine, a mitochondrial apoptosis-induced channel blocker. It inhibited BAK activation by direct binding to BAK and blocking the oligomerization of BAK.