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- W2022331892 abstract "A kappa-opioid receptor subtype was purified from a digitonin solubilized preparation of frog brain membranes using affinity chromatography. The affinity resin was prepared by coupling D-Ala2-Leu3-enkephalin to Sepharose-6B matrix. After elution of the receptor by 50 μmol naloxone, the kappa-subtype was separated from the mu- and delta-subtypes by gel permeation chromatography on Sepharose-6B. The purified receptor binds 3,900 pmol [3H]-ethylketocyclazocine per mg protein (a 4,300-fold purification over the membrane-bound receptor) with a KD of 8.3 nM. The purified receptor protein exhibits high affinity for kappa-selective ligands. The purified fraction shows two bands (Mr 65,000 and 58,000) in sodium dodecyl sulfate gel electrophoresis." @default.
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- W2022331892 date "1987-07-01" @default.
- W2022331892 modified "2023-10-17" @default.
- W2022331892 title "Purification of a kappa-opioid receptor subtype from frog brain" @default.
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- W2022331892 doi "https://doi.org/10.1016/0143-4179(87)90085-0" @default.
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