Corticotropin and β-endorphin: Construction and analysis of recombinant DNA complementary to mRNA for the common precursor

J. L. Roberts, P. H. Seeburg, J. Shine, E. Herbert, J. D. Baxter, H. M. Goodman

Research output: Contribution to journalArticlepeer-review

88 Scopus citations

Abstract

A cDNA fragment synthesized from mouse mRNA (ACTH/LPH mRNA) that codes for the precursor polypeptide containing corticotropin (ACTH), β-lipoprotein (LPH), and several other peptides has been cloned in bacteria. The mRNA was enriched for ACTH/LPH mRNA translational activity (to about 75%) prior to cDNA synthesis. It appears to contain about 1200 bases, of which approximately 450 bases are not translated. The cloned DNA fragment is complementary to the region of the mRNA coding for the protein fragment β-LPH-(44-90); this contains all of the amino acids of [Met]-enkephalin (residues 61-65 of β-LPH), most of the amino acids of β-melanocyte-stimulating hormone, and all but the carboxy-terminal amino acid of β-endorphin. Based on assignment of the amino acid sequence of mouse β-LPH from the nucleic acid sequence, it appears that there is extensive homology of mouse β-LPH with human and porcine β-LPH. The data also establish the linkage between β-melanocyte-stimulating hormone and β-endorphin as a Lys-Arg sequence. It is hoped that this cloned DNA can be used as a probe to study the expression and structure of the ACTH/LPH gene.

Original languageEnglish (US)
Pages (from-to)2153-2157
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number5
DOIs
StatePublished - 1979

ASJC Scopus subject areas

  • General

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