title: First biochemical characterization of a novel ribonuclease from wild mushroom Amanita hemibapha.
abstract: A 45-kDa ribonuclease (RNase) was purified from dried fruiting bodies of the wild mushroom Amanita hemibapha. It was adsorbed on DEAE-cellulose, S-sepharose, and finally purified on Superdex 75. The RNase exhibited maximal RNase activity at pH 5 and in a temperature range between 60-70°C. It demonstrated no ribonucleolytic activity toward four polyhomoribonucleotides. The amino acid sequence analysis (GDDETFWEHEWAK) showed this RNase was a ribonuclease T2-like RNase. It exhibited strong inhibitory activity against HIV-1 reverse transcriptase (HIV-1 RT) with an IC(50) of 17 μM.
authors: State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, 100193 China.
authors: Malota
authors: M
authors: Sekete
authors: Duanzheng
authors: D
authors: Ma
authors: Bo
authors: B
authors: Wang
authors: Hexiang
authors: H
authors: Wang
authors: Tzibun
authors: T
authors: Ng
keywords: Mushroom; Purification; Ribonuclease