Isolation, structure and synthesis of a heptapeptide with in vitro ACTH-releasing activity from porcine hypothalamus.
Significant CRF activity was found in a fraction with Rf = 0.82-0.7 or VE/VT = 0.41-0.48 obtained by gel filtration of acid extracts of pig hypothalami on Sephadex G-25. The activity of this fraction decreased markedly during subsequent purification, particularly in the last two steps. From this fraction, a heptapeptide with significant ACTH releasing activity in vitro, was isolated in pure state, and its amino acid sequence was established as H-Phe-Ile-Tyr-His-Ser-Tyr-Lys-OH. This heptapeptide was synthesized by solid phase methods. The CRF activity of synthetic heptapeptide in vitro was low but could be potentiated by a cofactor fraction from rat hypothalamic extract.
D000324:Adrenocorticotropic Hormone / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D003346:Corticotropin-Releasing Hormone / Q000032:analysis / Q000302:isolation & purification*; D007031:Hypothalamus / Q000032:analysis*; D010455:Peptides / Q000138:chemical synthesis / Q000302:isolation & purification*; D013552:Swine
D010455:Peptides; D000324:Adrenocorticotropic Hormone; D003346:Corticotropin-Releasing Hormone