α-Neo-endorphin: Receptor binding properties of the tritiated ligand Article

Houghten, RA, Bartlett, SM, Ostresh, JM. (1983). α-Neo-endorphin: Receptor binding properties of the tritiated ligand . LIFE SCIENCES, 33(18), 1811-1820. 10.1016/0024-3205(83)90689-6

cited authors

  • Houghten, RA; Bartlett, SM; Ostresh, JM

authors

abstract

  • Tritiated porcine α-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 α-neo-endorphin having a specific activity of 45.5 Ci/mmole. Both the native, iodinated and tritiated α-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 α-neo-endorphin to rat membrane preparations is described using [3H2Tyr1]α-neo-endorphin as the ligand. The binding is time-dependent and saturable with respect to α-neo-endorphin. Scatchard analysis was bi-phasic with KDs of 0.20 and 3.75 nM. Displacement binding studies indicate that the receptor for α-neo-endorphin has "kappa" and possibly "epsilon" binding characteristics. © 1983.

publication date

  • October 31, 1983

published in

Digital Object Identifier (DOI)

start page

  • 1811

end page

  • 1820

volume

  • 33

issue

  • 18