Primary structure and biological activity of bradykinin potentiating peptides from Bothrops insularis snake venom.
Several bradykinin potentiating peptides (BPPs) were isolated from the venom of the Brazilian arboricole snake Bothrops insularis by gel filtration on Sephadex G-150-120, followed by sequencial high-voltage paper electrophoreses at pH 3.5, 6.5, and 2.1. The BPPs were assayed by their ability to potentiate the contractile activity, on the isolated guinea pig ileum, and the hypotensive activity, on anesthetized rats, of bradykinin. Eight BPPs, containing 3-13 amino acid residues, were sequenced and their primary structures were shown to have a marked degree of homology with those of several BPPs from other venoms.
Cintra
A C
AC
Departamento de Bioquímica, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Brasil.
Vieira
C A
CA
Giglio
J R
JR
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D004305:Dose-Response Relationship, Drug; D004590:Electrophoresis, Paper; D006168:Guinea Pigs; D006863:Hydrogen-Ion Concentration; D007082:Ileum / Q000187:drug effects; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000302:isolation & purification*; D051381:Rats
D003435:Crotalid Venoms; D009842:Oligopeptides; C006791:bradykinin potentiating factors