Blomhotin: a novel peptide with smooth muscle contractile activity identified in the venom of Agkistrodon halys blomhoffii

• Published in: Toxicon (Oxford) Vol. 37; no. 12; pp. 1761 - 1770
• Main Authors: Yanoshita, R., Kasuga, A., Inoue, S., Ikeda, K., Samejima, Y.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.12.1999; Elsevier Science
• Subjects: Agkistrodon halys blomhoffii; Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Animals; Biological and medical sciences; blomhotin; Chromatography, Gel; Chromatography, High Pressure Liquid; Crotalid Venoms - chemistry; Dose-Response Relationship, Drug; Gastric Fundus - drug effects; Male; Mass Spectrometry; Medical sciences; Molecular Sequence Data; Muscle Contraction - drug effects; Muscle, Smooth - drug effects; Oligopeptides - isolation & purification; Oligopeptides - pharmacology; Rats; Rats, Wistar; Toxicology; Viperidae; Purification; Peptides; Toxicity; Animal origin; Smooth muscle; Biological activity; Contraction; Ophidia; Vertebrata; Venom; Isolation; Reptilia; Aminoacid sequence; Structural analysis
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/S0041-0101(99)00117-8

A novel peptide has been isolated from the venom of Agkistrodon halys blomhoffii using a bioassay that monitors the stimulant effect on rat stomach fundus. The 11-amino acid peptide, named blomhotin, was purified to homogeneity by gel-filtration column chromatography and reverse-phase HPLC. The amino acid sequence of blomhotin was determined to be pGlu-Gly-Arg-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Arg, which is similar to that of bradykinin-potentiating peptides which themselves cause no contraction of smooth muscle. The contraction induced by blomhotin showed homologous desensitization, implicating the involvement of a blomhotin-specific site in the response.