6533b851fe1ef96bd12a8f72
RESEARCH PRODUCT
Isolation of the Endothelin B Receptor from Bovine Lung Structure, Signal Sequence, and Binding Site
Ina HeidemannSimone HickWerner Müller-esterlJasminka Godovac-zimmermannJasminka Godovac-zimmermannVukic SoskicVukic Soskicsubject
Binding SitesDNA ComplementaryEndothelin receptor type AReceptors EndothelinEndothelinsMolecular Sequence DataBiologyReceptor Endothelin BBiochemistryEndothelin 1Molecular biologyChromatography AffinityBiochemistrycardiovascular systemEnzyme-linked receptorAnimalsCattleElectrophoresis Polyacrylamide Gel5-HT5A receptorAmino Acid SequenceBinding siteGABBR1Endothelin receptorLungProtease-activated receptor 2description
Bovine lung endothelin-B receptor has been isolated in good yield with a new procedure involving the use of endothelin-1 coupled to iminobiotin with a long spacer and avidin-agarose affinity chromatography. Contrary to previous reports, evidence has been obtained that the native form of this receptor corresponds to the full-length transcript expected on the basis of cDNA clones. The binding of endothelin to a variety of shortened fragments of the full receptor suggests that the long N-terminal sequence of this receptor has very little influence on the binding of endothelin and that the main determinants of the endothelin binding site might be constituted by residues in the sixth, and possibly the seventh, transmembrane helices.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1995-11-15 | European Journal of Biochemistry |