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