SRTX‐d, a new native peptide of the endothelin/sarafotoxin family
- 9 October 1989
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 256 (1-2) , 1-3
- https://doi.org/10.1016/0014-5793(89)81706-5
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.Sarafotoxin; Endothelin; Snake venom; AortKeywords
This publication has 7 references indexed in Scilit:
- Vasoconstrictor effects of sarafotoxins in rabbit aorta: Structure-function relationshipsBiochemical and Biophysical Research Communications, 1989
- Similarities in mode and sites of action of sarafotoxins and endothelinsTrends in Pharmacological Sciences, 1989
- Structure-activity relationships of endothelin: Importance of the C-terminal moietyBiochemical and Biophysical Research Communications, 1988
- A novel potent vasoconstrictor peptide produced by vascular endothelial cellsNature, 1988
- Sarafotoxins S6: Several isotoxins from Atractaspis engaddensis (burrowing asp) venom that affect the heartToxicon, 1988
- A new type of toxin in the venom of snakes of the genus Atractaspis (Atractaspidinae)Toxicon, 1982
- The Chromatographic Determination of Cystine and Cysteine Residues in Proteins as S-β-(4-Pyridylethyl)cysteineJournal of Biological Chemistry, 1970