Related Experiment Videos
SRTX-d, a new native peptide of the endothelin/sarafotoxin family
A Bdolah1, Z Wollberg, G Fleminger
1Department of Zoology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
FEBS Letters
|October 9, 1989
Abstract:
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.