Studies on bradykinin potentiating peptide (BPP) from venom of Zhejiang pit viper (Agkistrodon halys pallas)--relationship between structure and function of BPP.
The structure of the bradykinin potentiating peptide component BPP1 from a 70% methanol extract of the lyophilized powder of pit viper from Zhejiang Province is shown as follows: (formula see text) When the pyroglutamyl residue was removed by pyroglutamate aminopeptidase, the activity of BPP1 was enhanced two-fold but decreased gradually during the course of Edman degradation. The above facts show that the structure integrity of the C-terminal is absolutely necessary for the activity of BPP1.
D000595:Amino Acid Sequence; D000818:Animals; D003435:Crotalid Venoms / Q000032:analysis*; D009842:Oligopeptides / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D003435:Crotalid Venoms; D009842:Oligopeptides; C006791:bradykinin potentiating factors