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Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family, from the venom of the burrowing asp Atractaspis bibroni
Author(s) -
Becker Andreas,
Dowdle Eugene B.,
Hechler Ulrike,
Kauser Katalin,
Donner Peter,
Schleuning Wolf-Dieter
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81142-m
Subject(s) - endothelins , endothelin receptor , venom , peptide , vasoconstriction , receptor , peptide sequence , gene isoform , biology , stereochemistry , microbiology and biotechnology , medicine , endocrinology , biochemistry , chemistry , gene
A new member of the endothelin/sarafotoxin family of vasoconstrictor peptides, bibrotoxin (BTX), was isolated from the venom of the burrowing asp Atractaspis bibroni by reversed‐phase FPLC. The amino acid sequence of BTX differs from SRTX‐b in the substitution Ala 4 instead of Lys 4 , which suggests that it represents the peptide isoform of Atractaspis bibroni corresponding to SRTX‐b. BTX competed for [ 125 I]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.