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  • Title: A novel ribonuclease with HIV-1 reverse transcriptase inhibitory activity purified from the fungus Ramaria formosa.
    Author: Zhang R, Tian G, Zhao Y, Zhao L, Wang H, Gong Z, Ng TB.
    Journal: J Basic Microbiol; 2015 Feb; 55(2):269-75. PubMed ID: 24523258.
    Abstract:
    A purification protocol that encompassed anion exchange chromatography (EC) on DEAE-cellulose, cation EC on CM-cellulose, anion EC on Q-Sepharose, and fast protein liquid chromatography-gel filtration of Superdex 75 was used to isolate a ribonuclease from dried fruiting bodies of Ramaria formosa. The ribonuclease was unadsorbed on CM-cellulose but adsorbed on both DEAE-cellulose and Q-Sepharose. It displayed a molecular mass of 29-kDa in both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The ranking of its ribonucleolytic activity toward polyhomoribonucleotides was poly(U) > poly(C) > poly(G) > poly(A). It exhibited a pH optimum of pH 5 and a temperature optimum at 60 °C. The ribonuclease inhibited HIV-1 reverse transcriptase with an IC50 of 3 µM.
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