マサバ普通肉のカテプシンBの精製と性状

DOI 日本農学文献記事索引 Web Site 被引用文献3件

書誌事項

タイトル別名
  • Purification and characterization of cathepsin B from ordinary muscle of common mackerel Scomber japonicus.
  • マサバ普通肉のカテプシンBの精製と性状〔英文〕
  • マサバ フツウ ニク ノ カテプシン B ノ セイセイ ト セイジョウ エイブ

この論文をさがす

抄録

Cathepsin B (EC 3.4.22.1) was purified from the ordinary muscle of common mackerel by ammonium sulfate fractionation and successive chromatographies on Sephadex G-75, DEAE-Sepharose, CM-Sepharose, Q-Sepharose, and Sephacryl S-100 HR.<br>The purified enzyme showed a single protein band on polyacrylamide gel electrophoresis, and its molecular weight was estimated to be 23, 000 by SDS-polyacrylamide gel electrophoresis and gel filtration on Sephacryl S-200 HR. The optimal pH of the enzyme for the hydrolysis of Z-Arg-Arg-NMec was 5.5. The enzyme was activated by sulfhydryl compounds, such as 2-mercapto-ethanol, cysteine, dithiothreitol, and glutathione. Among the compounds, cysteine was the most effective. The enzyme was moderately inhibited by pCMB and NEM, and strongly inhibited by TLCK, TPCK, antipain, leupeptin, E-64, Cu2+, and He2+. The enzyme hydrolyzed Z-Phe-Arg-NMec and Bz-Arg-NNap, but not Arg-NMec or Leu-NNap. The ratio of hydrolyzing activity against Z-Phe-Arg-NMec and Z-Arg-Arg-NMec was about 1:0.7.

収録刊行物

  • 日本水産学会誌

    日本水産学会誌 55 (12), 2185-2190, 1989

    公益社団法人 日本水産学会

被引用文献 (3)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ