A Novel Ribonuclease with HIV-1 Reverse Transcriptase Inhibitory Activity Purified from the Field Blewit Mushroom Lepista personata (Agaricomycetes)
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AbstractA ribonuclease was purified from dry fruiting bodies of the wild edible mushroom Lepista personata (LPR) to 259-fold with a specific activity of 280 U/mg. The purification protocol involved ion-exchange chromatography on DEAE-cellulose, CM-cellulose and SP-sepharose, followed by size exclusion chromatography on Superdex 75. LPR is a homodimeric protein with a molecular weight of 27.8 kDa as determined by SDS-PAGE and by gel filtration. Three inner peptide sequences for LPR were obtained by LC-MS-MS analysis. It demonstrated the optimum pH of 4.0 and temperature optimum of 60°C. The specificity ribonuclease potencies order toward polyhomoribonucleotides was poly C > poly A > poly G > poly U. The ribonuclease inhibited HIV-1 reverse transcriptase with an IC50 of 0.53 μM.
All Author(s) ListLijing Xu, Xueran Geng, Mingchang Chang, Junlong Meng, Hexiang Wang, Tzi Bun Ng
Journal nameInternational Journal of Medicinal Mushrooms
Year2020
Month10
Volume Number22
Issue Number10
Pages991 - 1000
ISSN1940-4344
LanguagesEnglish-United Kingdom
KeywordsLepista personata, ribonuclease, isolation, HIV-1 reverse transcriptase, medicinal mushrooms