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

  • Hisao Kato
  • Tomoji Suzuki
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 8)


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.


Amino Acid Composition Thioglycolic Acid Pyroglutamic Acid Partial Acid Hydrolysis Tryptic Hydrolysate 
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Copyright information

© Plenum Press, New York 1970

Authors and Affiliations

  • Hisao Kato
    • 1
  • Tomoji Suzuki
    • 1
  1. 1.Division of Plasma Proteins, Institute for Protein ResearchOsaka UniversityOsakaJapan

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