マサバ普通肉のカテプシンBの精製と性状
書誌事項
- タイトル別名
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- 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
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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
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- 日本水産学会誌
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日本水産学会誌 55 (12), 2185-2190, 1989
公益社団法人 日本水産学会
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詳細情報 詳細情報について
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- CRID
- 1390282681387646592
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- NII論文ID
- 130001544654
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- NII書誌ID
- AN00193422
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- ISSN
- 1349998X
- 00215392
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- NDL書誌ID
- 3655185
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- IRDB
- NDL
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