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- W2004419528 abstract "A novel proteinase A inhibitor was purified from Ganoderma lucidum. The purification was carried out by ethanol precipitation (50–80%), ACA44 gel filtration and Source 30Q anion exchange, respectively. The molecular mass of the inhibitor was 38 kDa as estimated via SDS-PAGE and gel filtration. Its carbohydrate content was up to 70%. β-Elimination revealed that the linkage between the glycan and the core protein backbone might be O-linkage. This inhibitor showed a remarkable heat stability. By investigating the interaction between this inhibitor and a variety of proteinases, it is indicated that the inhibitor was more specific against yeast proteinase A than other proteinases. The dissociation constants (Ki) and concentration required for 50% inhibition (IC50) for proteinase A were 2.7 × 10−6 M and 0.16 mg/ml, respectively." @default.
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- W2004419528 date "2005-02-01" @default.
- W2004419528 modified "2023-09-23" @default.
- W2004419528 title "Purification and characterization of a novel proteinase A inhibitor from Ganoderma lucidum by submerged fermentation" @default.
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- W2004419528 doi "https://doi.org/10.1016/j.enzmictec.2004.10.003" @default.
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