Purification and Properties of Tyrosinase Isozymes from the Gill of<i>Lentinus edodes</i>Fruiting Body

• KANDA Katsuhiro

• SATO Toshitsugu

• ISHII Shizuko

• ENEI Hitoshi

• EJIRI Shin-ichiro

書誌事項

タイトル別名

• Purification and Properties of Tyrosinase Isozymes from the Gill of Lentinus edodes Fruiting Body.

抄録

Six tyrosinase isozymes were purified from the browned gill of the fruiting body of Lentinus edodes by ammonium sulfate fractionation, DEAE-Sephacel and Q-Sepharose column chromatography, and partially denaturing SDS-PAGE. At the stop of Q-Sopharose column chromatography, two active fractions (A and B) were obtained. Each fraction was separated to three further fractions, A1, A2, and A3, and B1, B2, and B3, respectively, by partially denaturing SDS-PAGE. All these isozymes consisted of two types of polypeptides: α polypeptide (Aα or Bα) and either β (Aβ or Bβ) or γ polypeptide (Aγ or Bγ). The αpolypeptide contained the consensus amino acid sequence of the active site of known tyrosinases, which is considered to act as a catalytic subunit. From the results of peptide mapping and the amino acid composition, Aα and Bα polypeptides were considered to be different proteins. The kinetic properties of the purified tyrosinase isozymes differed greatly according to whether they contained β or γ polypeptide, indicating these polypeptides to be a possible regulatory subunit.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 60 (8), 1273-1278, 1996

  公益社団法人 日本農芸化学会

キーワード

• Lentinus edodes
• tyrosinase
• monophenoloxidase
• purification
• subunit

詳細情報

• CRID: 1390282681453306368
• NII論文ID: 110002678244
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.60.1273
• COI: 1:CAS:528:DyaK28XltlektLY%3D
• ISSN: 13476947
• ISSN: 09168451
• ISSN: http://id.crossref.org/issn/09168451
• PubMed: 8987542
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.60.1273
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可