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

A. Bdolah; Z. Wollberg; G. Fleminger; E. Kochva

doi:10.1016/0014-5793(89)81706-5

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 journal › Article › peer-review

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; Aorta.

Original language	English
Pages (from-to)	1-3
Number of pages	3
Journal	FEBS Letters
Volume	256
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(89)81706-5
State	Published - 9 Oct 1989

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

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; Aorta.",

author = "A. Bdolah and Z. Wollberg and G. Fleminger and E. Kochva",

year = "1989",

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doi = "10.1016/0014-5793(89)81706-5",

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TY - JOUR

T1 - SRTX-d, a new native peptide of the endothelin/sarafotoxin family

AU - Bdolah, A.

AU - Wollberg, Z.

AU - Fleminger, G.

AU - Kochva, E.

PY - 1989/10/9

Y1 - 1989/10/9

N2 - 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.

AB - 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.

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U2 - 10.1016/0014-5793(89)81706-5

DO - 10.1016/0014-5793(89)81706-5

M3 - מאמר

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VL - 256

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EP - 3

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-2

ER -

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

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