Isolation: analysis and properties of three bradykinin-potentiating peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom.
In the course of systematic investigations on low-molecular-weight compounds from the venom of Crotalidae and Viperidae, we have isolated and characterized at least three bradykinin-potentiating peptides (BPP-II, BPP-III, and BPP-V) from Bothrops neuwiedi venom by gel filtration on Sephadex G-25 M, Sephadex G-10 followed by HPLC. The peptides showed bradykinin-potentiating action on isolated guinea-pig ileum, for which the BPP-V was more active than of BPP-II, and BPP-III, rat arterial blood pressure, and a relevant angiotensin-converting enzyme (ACE) competitive inhibiting activity. The kinetic studies showed a Ki of the order of 9.7 x 10(-3) microM to BPP-II, 7 x 10(-3) microM to BPP-III, and 3.3 x 10(-3) microM to BPP-V. The amino acid sequence of the BPP-III has been determined to be pGlu-Gly-Gly-Trp-Pro-Arg-Pro-Gly-Pro-Glu-Ile-Pro-Pro, and the amino acid compositions of the BPP-II and BPP-V by amino acid analysis were 2Glu-2Gly-1Arg-4Pro-1Ile and 2Glu-2Gly-1Ser-3Pro-2Val-1Ile, with molecular weight of 1372, 1046, and 1078, respectively.
Ferreira
L A
LA
Laboratório de Bioquimica e Biofisica, Instituto Butantan, São Paulo, Brazil.
Galle
A
A
Raida
M
M
Schrader
M
M
Lebrun
I
I
Habermehl
G
G
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology; D000818:Animals; D001794:Blood Pressure / Q000187:drug effects; D017837:Bothrops; D006168:Guinea Pigs; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000187:drug effects; D051381:Rats; D014757:Viper Venoms / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; D010455:Peptides; D014757:Viper Venoms; C006791:bradykinin potentiating factors; D007703:Peptidyl-Dipeptidase A