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A novel ribonuclease with HIV‐1 reverse transcriptase inhibitory activity purified from the fungus Ramaria formosa

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.