The present paper was undertaken to investigate the existence of new cathepsin B in mackerel white muscle. The proteinase hydrolyzing Z-Arg-Arg-methylcoumarylamide was separated into two fractions (Peaks-1 and -2) from mackerel muscle by Q Sepharose Fast Flow ion exchange chromatography, followed by Cellulofine GC-200 gel filtration. The enzyme in Peak-1 strongly hydrolyzed Z-Arg-Arg-methylcoumarylamide, and that in Peak-2 hydrolyzed Z-Phe-Arg-Arg-and Bz-Phe-Val-Arg-methylcoumarylamides much more than Z-Arg-Arg-methylcoumarylamide. The enzyme in Peak-1 shared several properties with that in Peak-2 as follows; inhibition by leupeptin, antipain, PCMB, and HgCl₂, activation of sulfhydryl reagents, and degradation of hemoglobin and albumin. Consequently, both enzymes were found to be a cysteine proteinase that show some similarities to cathepsin B. Moreover, the proteinase in Peak-1 was suggested to be a new type of cathepsin B, judging from the result of synthetic substrate specificity.
雑誌名
三重大学生物資源学部紀要 = The bulletin of the Faculty of Bioresources, Mie University
巻
3
ページ
97 - 103
発行年
1990-02-28
ISSN
0915-0471
書誌レコードID
AN10073846
フォーマット
application/pdf
著者版フラグ
publisher
日本十進分類法
464
その他のタイトル
Existence of New Cathepsin B in Mackerel White Muscle
マサバ普通肉中のnewカテプシンＢの存在
AN100738460000309.pdf
(389.47KB)
