Abstract
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.
