Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family, from the venom of the burrowing asp Atractaspis bibroni

FEBS Letters

Donner, Peter¹  Becker, Andreas¹  Hechler, Ulrike¹  Schleuning, Wolf-Dieter¹  Kauser, Katalin¹  Dowdle, Eugene B.² 

[1] Research Laboratories of Schering AG, Berlin, Germany;Department of Clinical Science and Immunology, University of Cape Town Medical School, Cape Town, South Africa

关键词: Sarafotoxin;    Endothelin;    Snake venom;    Atractaspis bibroni;    ET;    endothelin;    SRTX;    sarafotoxin;    BTX;    bibrotoxin;    VIC;    vasointestinal contractor.;   

DOI  :  10.1016/0014-5793(93)81142-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new member of the endothelin/sarafotoxin family of vasoconstrictor peptides, bibrotoxin (BTX), was isolated from the venom of the burrowing aspAtractaspis bibroni by reversed-phase FPLC. The amino acid sequence of BTX differs from SRTX-b in the substitution Ala⁴ instead of Lys⁴, which suggests that it represents the peptide isoform of Atractaspis bibroni corresponding to SRTX-b. BTX competed for [¹²⁵I]ET-1 binding to human ET_B-type receptor with a K_i of 3.2 × 10⁻⁹ M compared to 4.2 × 10⁻⁹ M for SRTX-b. In rat thorax aorta BTX induced vasoconstrictions with a threshold concentration of 3 × 10⁻⁸ M compared to 1 × 10⁻⁹ for ET-1.

【 授权许可】

Unknown