SRTX-d, a new native peptide of the endothelin/sarafotoxin family.
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.
Bdolah
A
A
Department of Zoology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
Wollberg
Z
Z
Fleminger
G
G
Kochva
E
E
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000187:drug effects; D001665:Binding Sites; D002848:Chromatography, DEAE-Cellulose; D016232:Endothelins; D004730:Endothelium, Vascular / Q000032:analysis* / Q000187:drug effects; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D010455:Peptides / Q000032:analysis* / Q000633:toxicity; D011817:Rabbits; D012694:Serine / Q000032:analysis; D013912:Threonine / Q000032:analysis; D014662:Vasoconstrictor Agents / Q000032:analysis*; D014757:Viper Venoms / Q000494:pharmacology / Q000633:toxicity
D016232:Endothelins; D010455:Peptides; D014662:Vasoconstrictor Agents; D014757:Viper Venoms; C057354:sarafotoxins s6; D013912:Threonine; D012694:Serine