マダコ肝臓のカテプシンA,BおよびCの存在について

概要

論文の詳細を見る
In the previous paper dealing with the properties of the proteolytic enzyme from the liver of octopus, Octopus vulgaris CUVIER, it was shown that the action of the partially purified enzyme preparation on three synthetic substrates, such as carbobenzoxy-L-glutamyl-L-tyrosine (CGT, a substrate of cathepsin A), benzoyl-L-argin-inamide (BAA, a substrate of cathepsin B) and glycyl-L-phenylalaninamide (GPA, a substrate of cathepsin C), was detected. The data of the present investigation suggest that the enzyme action is due to the actions of cathepsins A, B and C. Thus it may be concluded that cathepsins A, B and C are present in the liver of octopus. These cathepsins A, B and C have optimal hydrolytic activities at near pH 5.0 on CGT, BAA and GPA, respectively, and their activities were high in the order B > A > C.
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