Isolation and characterization of a bradykinin potentiating peptide (BPP-S) isolated from Scaptocosa raptoria venom

Venom of the spider Scaptocosa raptoria was fractionated by chromatography on Sephadex G-10 followed by HPLC, and a bradykinin potentiating peptide, BPP-S, was obtained in pure form. The amino acid sequence of this undecapeptide is presented. Peptide BPP-S significantly potentiates the effects of br...

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Veröffentlicht in:	Toxicon (Oxford) 1996-05, Vol.34 (5), p.599-603
Hauptverfasser:	Ferreira, L.A.F., Alves, W.E., Lucas, M.S., Habermehl, G.G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Angiotensin-Converting Enzyme Inhibitors - pharmacology Animal poisons toxicology. Antivenoms Animals Araneae Biological and medical sciences Bothrops Bradykinin - chemistry Bradykinin - isolation & purification Bradykinin - metabolism Chemical Fractionation Chromatography, High Pressure Liquid Crotalid Venoms - chemistry Crotalid Venoms - metabolism Dose-Response Relationship, Drug Lycosidae Medical sciences Muscle Contraction - drug effects Muscle, Smooth - drug effects Oligopeptides - chemistry Oligopeptides - isolation & purification Oligopeptides - metabolism Oligopeptides - pharmacology Scaptocosa raptoria Toxicology
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Zusammenfassung:	Venom of the spider Scaptocosa raptoria was fractionated by chromatography on Sephadex G-10 followed by HPLC, and a bradykinin potentiating peptide, BPP-S, was obtained in pure form. The amino acid sequence of this undecapeptide is presented. Peptide BPP-S significantly potentiates the effects of bradykinin on smooth muscle, and inhibits the angiotensin-converting enzyme (ACE) in vitro.
ISSN:	0041-0101 1879-3150
DOI:	10.1016/0041-0101(96)00010-4