A Novel Ribonuclease with HIV-1 Reverse Transcriptase Inhibitory Activity Purified from the Field Blewit Mushroom Lepista personata (Agaricomycetes).
Int J Med Mushrooms
; 22(10): 991-1000, 2020.
Article
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| MEDLINE
| ID: mdl-33426828
ABSTRACT
A 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.
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Bases de datos:
MEDLINE
Asunto principal:
Ribonucleasas
/
Proteínas Fúngicas
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Agaricales
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Transcriptasa Inversa del VIH
Idioma:
En
Revista:
Int J Med Mushrooms
Año:
2020
Tipo del documento:
Article