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Separation of κ‐opioid receptor subtype from frog brain
Author(s) -
Simon József,
Benyhe Sándor,
Borsodi Anna,
Szücs Mária,
Wollemann Mária
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80818-8
Subject(s) - digitonin , stokes radius , sedimentation coefficient , enkephalin , receptor , chemistry , κ opioid receptor , δ opioid receptor , stereochemistry , chromatography , membrane , biochemistry , enzyme , opioid
Complete separation of the [ 3 H]ethylketocyclazocine ([ 3 H]EKC) specific binding (k subtype) from tritiated Tyr‐D‐Ala 2 ‐Me‐Phe 4 ‐Gly‐ol 5 enkephalin (DAGO) and Tyr‐D‐Ala 2 ‐L‐Leu 5 ‐enkephalin (DALA) binding (μ‐and δ‐subtypes, respectively) was achieved by Sepharose‐6B chromatography and sucrose density gradient centrifugation of digitonin solubilized frog brain membranes. The apparent sedimentation coefficient ( S 20 ,w) for the k receptor‐detergent complex was 13.1 S and the corresponding Stokes radius 64 Å. The isolated fractions exhibited high affinity for EKC and bremazocine, whereas μ‐ and δ‐specific ligands were unable to compete for the [ 3 H]EKC binding sites, indicating that the κ subtype represents a separate molecular entity from the μ and δ receptor sites.