[Purification and properties of a hypothalamic peptide inhibiting prolactin secretion in vitro].
A pure preparation of a peptide inhibiting at low (nm-pcm) concentrations a de novo synthesis of prolactin and its secretion into the medium during incubation of rat adenohypophysial tissue has been isolated from cattle hypothalamus. The biological action of the inhibitor differs from that of the already known inhibitors of adenohypophysial hormone secretion--dophamine and somatostatin. The loss of activity by the preparation after treatment with chymotrypsin is indicative of a peptide nature of the inhibitor. The amino acid composition and the N-terminal sequence of the peptide demonstrate its structural similarity to Leu-enkephaline.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004298:Dopamine / Q000494:pharmacology; D004745:Enkephalins; D007028:Hypothalamic Hormones / Q000302:isolation & purification / Q000494:pharmacology*; D010903:Pituitary Gland, Anterior / Q000187:drug effects / Q000378:metabolism*; D010905:Pituitary Hormone Release Inhibiting Hormones / Q000302:isolation & purification / Q000494:pharmacology*; D011388:Prolactin / Q000378:metabolism*; D051381:Rats; D013004:Somatostatin / Q000494:pharmacology
D004745:Enkephalins; D007028:Hypothalamic Hormones; D010905:Pituitary Hormone Release Inhibiting Hormones; D013004:Somatostatin; D011388:Prolactin; D004298:Dopamine
Ochistka i svoĭstva gipotalamicheskogo peptida, ingibiruiashchego sekretsiia prolaktina in vitro.