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  • Title: Preparation and properties of tritiated human [Tyr18, Trp27]-beta-endorphin.
    Author: Hammonds RG, Li CH.
    Journal: Int J Pept Protein Res; 1985 Feb; 25(2):149-54. PubMed ID: 2985518.
    Abstract:
    Tritiated [Tyr18, Trp27]-beta h-EP was prepared from the corresponding diiodotyrosine derivative by catalytic reduction in the presence of carrier free tritium gas. A photoaffinity probe for beta-endorphin (beta-EP) receptors was prepared by selective modification of [Tyr18, Trp27]-beta h-endorphin with 2-nitro-4-azidophenylsulfenyl chloride (2,4-NAPS-C1) under acidic conditions to yield [Trp18-2,4-NAPS-Trp27]-beta h-endorphin (NAPS-beta-EP). NAPS-beta-EP was purified by high performance liquid chromatography and characterized by ultraviolet absorption spectroscopy and peptide mapping. Tritiated NAPS-beta-EP was prepared from tritiated [Tyr18, Trp27]-beta h-endorphin with 2,4-NAPS-C1. The ability of NAPS-beta-EP to form covalent bonds to macromolecules due to photolysis was established using bovine serum albumin. The efficiency of photolytic cross-linking was 15% and the equilibrium dissociation constant was 1.3 X 10(-5) M.
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