Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family, from the venom of the burrowing asp Atractaspis bibroni.
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 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 ETB-type receptor with a Ki of 3.2 x 10(-9) M compared to 4.2 x 10(-9) M for SRTX-b. In rat thorax aorta BTX induced vasoconstrictions with a threshold concentration of 3 x 10(-8) M compared to 1 x 10(-9) for ET-1.
Becker
A
A
Research Laboratories of Schering AG, Berlin, Germany.
Dowdle
E B
EB
Hechler
U
U
Kauser
K
K
Donner
P
P
Schleuning
W D
WD
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D016232:Endothelins / Q000737:chemistry; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D016415:Sequence Alignment; D014662:Vasoconstrictor Agents; D014757:Viper Venoms / Q000737:chemistry*
D016232:Endothelins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D014662:Vasoconstrictor Agents; D014757:Viper Venoms; C078887:bibrotoxin