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- W1413080728 abstract "The arginine deiminase (ADI, E.C 3.5.3.6) - a key enzyme of ADI pathway of Enterococcus faecium GR7 was purified to homogeneity. A sequential purification strategy involving ammonium sulfate fractionation, molecular sieve followed by Sephadex G-100 gel filtration was applied to the crude culture filtrate to obtain a pure enzyme preparation. The enzyme was purified with a fold of 16.92 and showed a final specific activity of 76.65IU/mg with a 49.17% yield. The dimeric ADI has a molecular mass of about 94,364.929Da, and comprises of hetrodimers of 49.1kDa and 46.5kDa as determined by MALDI-TOF and PAGE analysis. To assess anti-cancerous activity of ADI by MTT assay was carried out against cancer cell lines (MCF-7, Sp2/0-Ag14 and Hep-G2). Purified ADI exhibited the most profound antiproliferative activity against Hep-G2 cells; with half-maximal inhibitory concentration (IC50) of 1.95μg/ml. Purified ADI from E. faecium GR7 was observed to induce apoptosis in the Hep-G2 cells by DNA fragmentation assay. Our findings suggest the possibility of a future use of ADI from E. faecium GR7 as a potential anticancer drug." @default.
- W1413080728 created "2016-06-24" @default.
- W1413080728 creator A5033042716 @default.
- W1413080728 creator A5051579616 @default.
- W1413080728 date "2016-09-01" @default.
- W1413080728 modified "2023-09-24" @default.
- W1413080728 title "Purification of a dimeric arginine deiminase from Enterococcus faecium GR7 and study of its anti-cancerous activity" @default.
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- W1413080728 doi "https://doi.org/10.1016/j.pep.2015.09.011" @default.
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