Structure of Bradykinin Potentiating Peptides from the Venom of Agkistrodon halys blomhoffii

Abstract

It has recently been shown that the contractile action of bradykinin on isolated smooth muscles is potentiated by various substances. Ferreira and Rocha e Silva reported that chemical reagents, such as dimercaprol, cysteine and thioglycolic acid potentiate the bradykinin action (FERREIRA and ROCHA E SILVA, 1962). Edery found that proteolytic enzyme, such as chymotrypsin and trypsin sensitize smooth muscle to bradykinin (EDERY, 1965). Bradykinin potentiating activity of a tryptic hydrolysate of denatured human plasma was found by Aarsen (AARSEN, 1968), and Hamberg (HAMBERG et al., 1968), independently. Osbahr et al. also reported that some fibrinopeptides have bradykinin potentiating activity on isolated rat uterus (OSBAHR et al., 1964). In 1965, Ferreira found that the bradykinin potentiating factors in the venom of Bothrops jararaca seem to be peptide-like substances which are dialyzable and heat stable (FERREIRA, 1965). The authors also found the similar factors in the venom of Agkistrodon halys blomhoffii (Japanese name, Mamushi) (SUZUKI et al., 1967). In this communication, the isolation method of the bradykinin potentiating factors from the venom of A. halys blomhoffii has been established and structural studies on one of the potentiators have been undertaken.