Characterization of a 41-Residue Ovine Hypothalamic Peptide That Stimulates Secretion of Corticotropin and β-Endorphin
- 18 September 1981
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 213 (4514), 1394-1397
- https://doi.org/10.1126/science.6267699
Abstract
A peptide with high potency and intrinsic activity for stimulating the secretion of ACTH-like and .beta.-endorphin-like immunoactivities by cultured rat anterior pituitary cells was purified from ovine hypothalamic extracts. The primary structure of this 41-residue ACTH- and .beta.-endorphin-releasing factor is given. The synthetic peptide is active in vitro and in vivo.This publication has 25 references indexed in Scilit:
- Isolation and sequence analysis of a somatostatin-like polypeptide from ovine hypothalamusBiochemistry, 1981
- Active polypeptides: from amphibian skin to gastrointestinal tract and brain of mammalsTrends in Pharmacological Sciences, 1980
- β-endorphin concentration in the brain of intact and hypophysectomized ratsLife Sciences, 1979
- Corticotrophin releasing factor may be modulated vasopressinNature, 1979
- Isolation of N-acetylaspartic acid from hypothalamic tissue and significance of its ACTH-releasing activityBiochemical and Biophysical Research Communications, 1978
- STUDIES ON THE NATURE OF CORTICOTROPHIN RELEASING HORMONE AND ITS PARTIAL PURIFICATION FROM PORCINE HYPOTHALAMIJournal of Endocrinology, 1976
- Solid Phase Peptide Synthesis. I. The Synthesis of a TetrapeptideJournal of the American Chemical Society, 1963
- Evidence for the Existence of Two Corticotrophin-releasing Factors, α and βNature, 1960
- THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATEThe Journal of Experimental Medicine, 1957