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- W1990235696 abstract "Tritiated porcine alpha-neo-endorphin has been prepared from its corresponding iodinated analog. The iodinated analog (diiodotyrosine at position 1) was synthesized, along with its non-iodinated counterpart, by the solid-phase method. Catalytic exchange of this iodinated analog in the presence of tritium yielded tritiated porcine alpha-neo-endorphin having a specific activity of 45.5 Ci/mmole. Both the native, iodinated and tritiated alpha-neo-endorphin analogs were shown to be homogenous by chromatography on carboxymethylcellulose, paper chromatography, paper electrophoresis, high performance liquid chromatography and amino acid analysis. For the first time binding of alpha-neo-endorphin to rat membrane preparations is described using [3H2-Tyr1]alpha-neo-endorphin as the ligand. The binding is time-dependent and saturable with respect to alpha-neo-endorphin. Scatchard analysis was bi-phasic with KDs of 0.20 and 3.75 nM. Displacement binding studies indicate that the receptor for alpha-neo-endorphin has kappa and possibly epsilon binding characteristics." @default.
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- W1990235696 date "1983-10-01" @default.
- W1990235696 modified "2023-10-16" @default.
- W1990235696 title "α-Neo-endorphin: Receptor binding properties of the tritiated ligand" @default.
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- W1990235696 doi "https://doi.org/10.1016/0024-3205(83)90689-6" @default.
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