BETA-ENDORPHIN - RADIORECEPTOR BINDING ASSAY - RELATIVE POTENCY OF SYNTHETIC ANALOGS WITH VARIOUS CHAIN LENGTHS

  • 1 January 1980
    • journal article
    • research article
    • Vol. 16  (1) , 66-69
Abstract
An assay system is described to measure the specific binding of .beta.-endorphin to opiate sites (receptors) in rat brain membrane preparations using the tritiated hormone as the primary ligand. By this assay procedure, the radioreceptor activity of .beta.-endorphin and synthetic analogs [.beta.h-endorphin [EP], .beta.h-EP-(1-30), .beta.h-EP-(1-29), .beta.h-EP-(1-28), .beta.h-EP-(1-26), .beta.h-EP-(1-21), .beta.h-EP-(1-15), .beta.h-EP-(1-5) [Met-enkephalin] and .beta.c-EP-(6-31) (subscripts h and c indicate human and camel)] with various chain lengths was determined. The results suggest that both NH2- and COOH-terminal sequences of the molecule are involved in the interaction of .beta.-endorphin with opiate receptors.

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