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- W2103160275 abstract "An RNase with a molecular mass of 28 kDa and with high ribonucleolytic activity toward poly(A) was purified from the ascocarps of Tuber indicum . The purification procedure involved ion exchange chromatography on diethylaminoethyl cellulose, Q‐Sepharose and Mono Q, and gel filtration by fast protein liquid chromatography on Superdex 75. The pH and temperature optima of the RNase were 7.2 and 50 °C, respectively. The ranking of its activity toward various polyhomoribonucleotides was poly(A)>poly(C)>poly(G) ≈ poly(U). All of the metal ions used in this study, except for the K + ions, curtailed the activity of the RNase. The RNase activity was reduced by ethylene diamine tetraacetic acid (EDTA), dithiothreitol (DTT), and sodium dodecyl sulfate (SDS) by 42.2%, 75.5%, and 96.6%, respectively. The RNase inhibited the proliferation of hepatoma (HepG2) and human breast cancer cell lines (MCF7), with half‐maximal inhibitory concentrations (IC 50 ) of 12.6 and 16.6 μM, respectively." @default.
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- W2103160275 date "2013-06-21" @default.
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- W2103160275 title "Purification and characterization of a ribonuclease with antiproliferative activity from the mystical wild mushroom<i>Tuber indicum</i>" @default.
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- W2103160275 doi "https://doi.org/10.1002/jobm.201300018" @default.
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