マサバ普通肉中のnewカテプシンＢの存在

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  • マサバ フツウ ニクチュウ ノ new カテプシン B ノ ソンザイ

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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.

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