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- W2022671700 abstract "Cysteine protease activity in mycelial culture increased 7.7-fold after fruit body formation in Pleurotus ostreatus, using the Leu pNA (LPNA) cleavage assay. The enzyme was purified from fruit bodies and its Mr was 97,000 by gel filtration and 48,500 by SDS-PAGE, indicating that it is a dimer. The enzyme was sensitive to iodoacetic acid, p-chloromercuribenzoate, N-ethylmaleimide, and HgCl2. The sequence of the first 9 N-terminal amino acids of cysteine protease was ASGLXXAIL." @default.
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- W2022671700 date "1998-01-01" @default.
- W2022671700 modified "2023-09-26" @default.
- W2022671700 title "Purification and Characterization of Cysteine Protease fromPleurotus ostreatus" @default.
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- W2022671700 doi "https://doi.org/10.1271/bbb.62.1416" @default.
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