SRTX-d, a new native peptide of the endothelin/sarafotoxin family

A. Bdolah*, Z. Wollberg, G. Fleminger, E. Kochva

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

84 Scopus citations


The primary structure of a new sarafotoxin, SRTX-d, from the venom of Atractaspis engaddensis is described. SRTX-d differs from SRTX-b in two substitutions: Ile19 instead of Val and Thr2 instead of Ser. The toxicity of SRTX-d and its vasoconstriction potency are very low in comparison to SRTX-a and SRTX-b, whereas its IC50 for 125I-SRTX-b binding is similar to that of SRTX-b. It is suggested that the Thr to Ser substitution, which is shared by two additional weak members of the endothelin/sarafotoxin family, SRTX-c and ET-3, affects the biological activity of SRTX-d as well. Sarafotoxin; Endothelin; Snake venom; Aorta.

Original languageEnglish
Pages (from-to)1-3
Number of pages3
JournalFEBS Letters
Issue number1-2
StatePublished - 9 Oct 1989


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