A bradykinin potentiating peptide (BPP) was purified from the Chinese snake venom (Agkistrodon halys Pallas). The amino acid sequence of this BPP was determined to be pyroGlu-Gly-Arg-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro. Removal of the N-terminal residue with pyroglutamate aminopeptidase enhanced two-fold the activity of BPP, the resulting despyroGlu-BPP gradually lost its activity on further Edman degradation. However, around 90% of the original activity was still present in the C-terminal tripeptide Ile-Pro-Pro. Some analogs of this tripeptide were synthesized by the conventional method, and investigated by two biological assays, i.e., potentiating response on bradykinin (BK) and inhibitory activity on angiotensin converting enzyme (ACE). It was shown that the two biological activities inherent in the synthetic analogs were not parallel to each other. In addition, the isolated guinea pig ileum strips treated with chelating agent to irreversibly inactivate kininase (the same enzyme ACE) still responded to BPP. Consequently the potentiating effect of BPP on BK in vitro bioassay might be due to its influence on the binding receptor for BK rather than the inhibitory effect on kininase.