@article{oai:mie-u.repo.nii.ac.jp:00005700,
 author = {上野, 隆二 and Ueno, Ryuji and 池田, 誠司 and Ikeda, Seiji and 青木, 恭彦 and Aoki, Takahiko},
 journal = {三重大学生物資源学部紀要 = The bulletin of the Faculty of Bioresources, Mie University},
 month = {Feb},
 note = {application/pdf, 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.},
 pages = {97--103},
 title = {マサバ普通肉中のnewカテプシンＢの存在},
 volume = {3},
 year = {1990}
}