Abstract
Human endothelin B receptor and its domain-truncated forms were cloned and expressed in Pichia pastoris. Ligand binding studies with expressed proteins were carried out using biotinylated endothelins. Competitive binding and liposome incorporation studies showed that the extracellular region is essential for ligand binding and that longer peptides have higher affinity.
Keywords: Recombinant human endothelin B receptors, Pichia expression, synthetic peptides, competitive binding
Protein & Peptide Letters
Title: Endothelin and Its Receptor Interactions: Role of Extracellular Receptor Domain and Length of Peptide Ligands
Volume: 14 Issue: 8
Author(s): K. Saravanan, G. Hariprasad, O. Jitesh, U. Das, S. Dey, S. Sharma, P. Kaur, T.P. Singh and A. Srinivasan
Affiliation:
Keywords: Recombinant human endothelin B receptors, Pichia expression, synthetic peptides, competitive binding
Abstract: Human endothelin B receptor and its domain-truncated forms were cloned and expressed in Pichia pastoris. Ligand binding studies with expressed proteins were carried out using biotinylated endothelins. Competitive binding and liposome incorporation studies showed that the extracellular region is essential for ligand binding and that longer peptides have higher affinity.
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Cite this article as:
K. Saravanan , G. Hariprasad , O. Jitesh , U. Das , S. Dey , S. Sharma , P. Kaur , T.P. Singh and A. Srinivasan , Endothelin and Its Receptor Interactions: Role of Extracellular Receptor Domain and Length of Peptide Ligands, Protein & Peptide Letters 2007; 14 (8) . https://dx.doi.org/10.2174/092986607781483651
DOI https://dx.doi.org/10.2174/092986607781483651 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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