Purification and Characterization of Cysteine Protease from Pleurotus ostreatus

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概要

• 論文の詳細を見る

• 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 M_r 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 HgCl_2. The sequence of the first 9 N-terminal amino acids of cysteine protease was ASGLXXAIL.

• 社団法人日本農芸化学会の論文
• 1998-07-23

著者

• Choi Hye-seon

  Department Of Biological Sciences (bk21 Program) And Immunomodulation Research Center University Of

• Shin Hyun-hee

  Department Of Biological Sciences And The Immunomodulation Research Center University Of Ulsan

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