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• W178525939 abstract "Publisher Summary A novel potent vasoconstrictor peptide endothelin (ET) has been isolated from the supernatant of cultured porcine endothelial cells. Molecular cloning studies have revealed the existence of three distinct isoforms of ET—ET-1, ET-2, and ET-3—all containing 21 amino acid residues with two disulfide bonds. Autoradiographic studies of rat, porcine, and human tissues have indicated that ET receptors are present in the arteries and heart as well as in other nonvascular organs. The differential pharmacological profile of the ETs in the nonvascular tissues suggests that there are several ET receptor subtypes, and two subtypes of the ET receptors have been cloned. Results indicate that these receptors contain seven transmembrane domains and exhibit significant sequence similarity with other G-protein-coupled receptors. The high affinity constant between the glycoprotein avidin and the vitamin biotin provides an important experimental tool for a wide variety of biological applications. The avidin–biotin technique has been used to localize and purify various peptide hormone receptors, such as those for insulin, gonadotropin-releasing hormone, parathyroid hormone, corticotropin-releasing hormone, and vasopressin. This chapter discusses the synthesis and characterization of biotinylated ET analogs, and describes their potential utilization for the purification and localization of ET receptors." @default.
• W178525939 created "2016-06-24" @default.
• W178525939 creator A5067055601 @default.
• W178525939 creator A5077409232 @default.
• W178525939 date "1993-01-01" @default.
• W178525939 modified "2023-09-27" @default.
• W178525939 title "Biotinylated Endothelin Analogs as Probes for Endothelin Receptor" @default.
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• W178525939 doi "https://doi.org/10.1016/b978-0-12-185275-7.50013-5" @default.
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