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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 ?M.

SUBMITTER: Sekete M 

PROVIDER: S-EPMC3568466 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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First biochemical characterization of a novel ribonuclease from wild mushroom Amanita hemibapha.

Sekete Malota M   Ma Duanzheng D   Wang Bo B   Wang Hexiang H   Ng Tzibun T  

SpringerPlus 20121227 1


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 inhibito  ...[more]

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