ナマズの膵臓カルボキシペプチダーゼBの酵素の性質

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概要

• 論文の詳細を見る

• Two carboxypeptidases B from the pzncreas of the catfish Parasilurus asotus were found to have pH optima of 7.5 and were found to be stable between pH 6.5 and 9.0. Both enzymes were strongly inhibited by EDTA, o-phenanthroline, and cysteine. The enzymes inactivated by EDTA were regenerated almost completely by the addition of ZnCl2. These results indicate that both enzymes are metalloenzymes which require zinc for activity. Both enzymes were found to be able to hydrolyze Bz-Gly-Arg and Bz-Gly-Lys. These results indicate the close similarity between two catfish carboxypeptidases B and suggest that the catfish enzymes are closely related to carboxypeptidases B from other species.

• 公益社団法人 日本水産学会の論文

著者

• 吉中 禮二

  東京大学農学部水産学科

• 佐藤 守

  東京大学農学部水産学科

• 森下 丈二

  東京大学農学部水産学科

• 池田 静徳

  東京大学農学部水産学科

関連論文

• ナマズの膵臓カルボキシペプチダーゼBの酵素の性質

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