Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1978 Feb;75(2):669–671. doi: 10.1073/pnas.75.2.669

Characterization of pro-opiocortin, a precursor to opioid peptides and corticotropin.

M Rubinstein, S Stein, S Udenfriend
PMCID: PMC411317  PMID: 204928

Abstract

The high molecular weight (approximately 30,000) precursor to opioid activity (pro-opiocortin) previously detected in extracts of rat pituitary was digested with trypsin and the resulting peptide mixture was resolved by high-performance reverse-phase chromatography. A peak of opioid activity was eluted at the position of the nonapeptide beta-LPH (61-69), which was also the same fragment obtained by trypsin digestion of betas-lipotropin or beta-endorphin. This identified the protein as a precursor to the endorphins and Met-enkephalin. No activity was detected in the position corresponding to the Leu5 analog of betas-LPH (61-69), thus ruling out the possibility of a beta-lipotropin-like precursor to Leu-enkephalin in pituitary extracts. Pro-opiocortin and beta-lipotropin are present in rat pituitary extracts in comparable amounts, approximately 10 pmol/mg of tissue.

Full text

PDF
669

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chrétien M., Gilardeau C., Seidah N., Lis M. Purification and partial chemical characterization of human pituitary lipolytic hormone. Can J Biochem. 1976 Sep;54(9):778–782. doi: 10.1139/o76-111. [DOI] [PubMed] [Google Scholar]
  2. Gráf L., Li C. H. Action of plasmin on ovine beta-lipotropin: revision of the carboxyl terminal sequence. Biochem Biophys Res Commun. 1973 Aug 21;53(4):1304–1309. doi: 10.1016/0006-291x(73)90607-4. [DOI] [PubMed] [Google Scholar]
  3. Guillemin R., Vargo T., Rossier J., Minick S., Ling N., Rivier C., Vale W., Bloom F. beta-Endorphin and adrenocorticotropin are selected concomitantly by the pituitary gland. Science. 1977 Sep 30;197(4311):1367–1369. doi: 10.1126/science.197601. [DOI] [PubMed] [Google Scholar]
  4. Lohmar P., Li C. H. Isolation of bovine beta-lipotropic hormone. Biochim Biophys Acta. 1967 Oct 23;147(2):381–383. doi: 10.1016/0005-2795(67)90416-3. [DOI] [PubMed] [Google Scholar]
  5. Mains R. E., Eipper B. A., Ling N. Common precursor to corticotropins and endorphins. Proc Natl Acad Sci U S A. 1977 Jul;74(7):3014–3018. doi: 10.1073/pnas.74.7.3014. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Rubinstein M., Stein S., Gerber L. D., Udenfriend S. Isolation and characterization of the opioid peptides from rat pituitary: beta-lipotropin. Proc Natl Acad Sci U S A. 1977 Jul;74(7):3052–3055. doi: 10.1073/pnas.74.7.3052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Rubinstein M., Stein S., Udenfriend S. Isolation and characterization of the opioid peptides from rat pituitary: beta-endorphin. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4969–4972. doi: 10.1073/pnas.74.11.4969. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES