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2011 | 58 | 4 | 567-572
Article title

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

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EN
Abstracts
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.
Publisher

Year
Volume
58
Issue
4
Pages
567-572
Physical description
Dates
published
2011
received
2011-05-10
revised
2011-08-18
accepted
2011-12-05
(unknown)
2011-12-06
Contributors
author
  • State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, China
  • Institute of Biotechnology and Germplasmic Resource, Yunnan Academy of Agricultural Science, Kunming, China
author
  • Institute of Biotechnology and Germplasmic Resource, Yunnan Academy of Agricultural Science, Kunming, China
author
  • State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, China
author
  • School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv58p567kz
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