Abstract
Using the tritiated opiate antagonist [ 3H]naloxone, stereospecific opiate receptor binding was demonstrable in a bovine retina homogenate. Scatchard analysis of the saturation experiments revealed an apparent dissociation constant ( K D) of about 8·5 n m and a maximal number of binding sites ( B max) of about 0·24 pmol/mg protein. The properties of opiate receptor binding in bovine retina parallel those found in the rat brain. Agonist binding was altered by sodium ions. Subcellular distribution of stereospecific [ 3H]naloxone binding showed the highest density of binding sites in the P 1-fraction and high concentrations in the P 0- and P 2-fraction.
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