HUMAN β‐ENDORPHIN: SYNTHESIS AND CHARACTERIZATION OF ANALOGS IODINATED AND TRITIATED AT TRYOSINE RESIDUES 1 AND 27

RICHARD A. HOUGHTEN, WEN‐CHANG ‐C CHANG, CHOH HAO LI

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Three tritiated analogs of human β‐endorphin have been prepared from their corresponding iodinated analogs. The iodinated analogs (diiodotyrosine at positions 1, 27 or 1 and 27) were synthesized by the solid‐phase method and were found to have biological and physical properties which were altered when compared with the native molecule. Catalytic exchange of these iodinated analogs in the presence of tritium yielded tritiated human β‐endorphins having full biological activity and specific activity of 50–100 Ci/mmol. Both the iodinated and tritiated β‐endorphin analogs were shown to be homogeneous by chromatography on carboxymethylcellulose, partition chromatography, paper chromatography, amino acid analysis, electrophoresis, high performance liquid chromatography, and isoelectric focusing on polyacrylamide.

Original languageEnglish
Pages (from-to)311-320
Number of pages10
JournalInternational Journal of Peptide and Protein Research
Volume16
Issue number4
DOIs
Publication statusPublished - Jan 1 1980
Externally publishedYes

Keywords

  • guinea pig ileum assay
  • iodinated β‐endorphin
  • solid phase peptide synthesis
  • tritiated β‐endorphin

ASJC Scopus subject areas

  • Biochemistry

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