A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

• Autorzy: Sun J. , Zhao Y. , Chai H. , Wang H. , Ng T. B.
• Języki publikacji: EN

Abstrakty

EN

A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.

Słowa kluczowe

EN

alkaline protease; antiproliferative activity; fruiting body; wild mushroom; Amanita farinosa; purification; toxic hazard; poisonous fungi; poisonous fungi zob.tez poisonous mushroom

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2011
• Tom: 58
• Numer: 4
• Opis fizyczny: p.567-572,fig.,ref.

Twórcy

autor

Sun J.

• State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, China

autor

Zhao Y.

autor

Chai H.

autor

Wang H.

autor

Ng T. B.

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