Evolution of the sarafotoxin/endothelin superfamily of proteins.
Lethal factors and enzymes in the secretion from Duvernoy's gland of three colubrid snakes.
At least two of the snake species examined have toxic secretions that may be important during feeding by killing or weakening and helping to subdue the struggling prey.
Accumulation of some secretory enzymes in venom glands of Vipera palaestinae.
It is concluded that each of the enzymes is secreted at a rate independent of the other two; this pattern of secretion can best be described as nonparallel.
Sarafotoxins S6: several isotoxins from Atractaspis engaddensis (burrowing asp) venom that affect the heart.
SRTX‐d, a new native peptide of the endothelin/sarafotoxin family
A novel cardiotoxic polypeptide from the venom of Atractaspis engaddensis (burrowing asp): cardiac effects in mice and isolated rat and human heart preparations.
Sarafotoxins and endothelins: evolution, structure and function.
Cloning and sequence analysis of cDNAs encoding precursors of sarafotoxins. Evidence for an unusual "rosary-type" organization.
The evolutionary history of the sarafotoxin/endothelin/endothelin-like superfamily.
- G. Landan, A. Bdolah, Z. Wollberg, E. Kochva, D. Graur
- Biology, ChemistryJournal of Cardiovascular Pharmacology
In several lineages, the peptides have independently accumulated identical amino acid replacements in position 2, which supports the hypothesis that residue 2 is crucial to biological activity.