蓬莱柿 (Ficus carica var. HORAISHI) のプロティナーゼに関する研究(第4報)

Ficin A, B, CおよびDのキニナーゼ作用

抄録

Substrate specificities of Ficin A, B, C and D from Ficus carica var. HORAISHI were examined with bradykinin, dansylbradykinin and synthetic substrates. These enzymes showed kininase activity, but differed greatly in their specific activities. Kinins were not released from bovine plasma kininogen. These enzymes hydrolyzed dansylbradykinin at the site of Gly⁴-Phe⁵ and Phe⁵-Ser⁶, however, the processes of the hydrolysis differed among the enzymes. Toward synthetic substrates, a part of α-N-substituted dipeptides and tripeptide was hydrolyzed but dipeptides were not. From these results, it is suggested that Ficin A, B, C and D show kininase activity, have the same specificity toward dansylbradykinin, and similar specificity toward synthetic substrates.