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Competitive interaction between endothelin and sarafotoxin: Binding and phosphoinositides hydrolysis in rat atria and
1Department of Biochemistry, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel 69978.
Biochemical and Biophysical Research Communications
|January 16, 1989
Abstract:
Binding studies with the structurally similar vasoconstrictor peptides 125I-endothelin and 125I-sarafotoxin b, the former of mammalian origin and the latter derived from snake venom, reveal their mutually exclusive binding to rat atrium and various regions of the rat brain. In these tissues endothelin, like sarafotoxin, induces phosphoinositide hydrolysis which is in part Ca2+-independent. It is suggested that endothelins and sarafotoxins share common binding sites and mechanisms of action.