Nucleotide sequence of cloned cDNA for bovine corticotropin-β-lipotropin precursor
- 1 March 1979
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 278 (5703), 423-427
- https://doi.org/10.1038/278423a0
Abstract
The nucleotide sequence of a 1,091-base pair cloned cDNA insert encoding bovine corticotropin-β-lipotropin precursor mRNA is reported. The corresponding amino acid sequence indicates that the precursor protein consists of repetitive units and includes a third melanotropin sequence in its cryptic portion. Pairs of lysine and arginine residues separate the component peptides of the precursor.This publication has 53 references indexed in Scilit:
- Purification and Characterization of the Messenger RNA Coding for Bovine Corticotropin/β‐Lipotropin PrecursorEuropean Journal of Biochemistry, 1979
- Distribution of the Messenger RNA Coding for the Common Precursor of Corticotropin and β‐Lipotropin within the Bovine PituitaryEuropean Journal of Biochemistry, 1979
- Cell‐free translation product containing corticotropin and β‐endorphin encoded by messenger RNA from anterior lobe and intermediate lobe of bovine pituitaryFEBS Letters, 1977
- Characterization of a common precursor to corticotropin and beta-lipotropin: cell-free synthesis of the precursor and identification of corticotropin peptides in the molecule.Proceedings of the National Academy of Sciences, 1977
- Glucocorticoid effect on the level of corticotropin messenger RNA activity in rat pituitary.Proceedings of the National Academy of Sciences of the United States of America, 1977
- Common precursor to corticotropins and endorphinsProceedings of the National Academy of Sciences, 1977
- A large product of cell-free translation of messenger RNA coding for corticotropin.Proceedings of the National Academy of Sciences of the United States of America, 1976
- Isolation, primary structure, and synthesis of α-endorphin and γ-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activityProceedings of the National Academy of Sciences, 1976
- Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.Proceedings of the National Academy of Sciences of the United States of America, 1976
- Pituitary PeptideNature New Biology, 1973