Dynorphin in bovine adrenal medulla. II. Isolation, partial characterization and biological activity of two distinct molecules.
Two highly potent dynorphin-like peptides were isolated from bovine adrenal medulla by successive chromatography of an acid (HCl) extract on Sephadex G-10, carboxymethylcellulose, Sephadex G-50 and partition chromatography on Sephadex G-50. Amino acid analysis of both peptides revealed the presence of 24 amino acids including the composition of dynorphin-(1-13) and differing from each other only by a few residues. Both peptides were shown to have the same activity as dynorphin-(1-13) in the guniea pig ileum assay and reacted as well as dynorphin-(1-13) with a specific antibody (R-31) directed against the synthetic material.
D000313:Adrenal Medulla / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D001921:Brain / Q000187:drug effects; D002417:Cattle; D002850:Chromatography, Gel; D004399:Dynorphins; D004723:Endorphins / Q000302:isolation & purification* / Q000494:pharmacology; D006168:Guinea Pigs; D007082:Ileum / Q000187:drug effects; D008297:Male; D008970:Molecular Weight; D010446:Peptide Fragments / Q000494:pharmacology; D011863:Radioimmunoassay; D051381:Rats
D000596:Amino Acids; D004723:Endorphins; D010446:Peptide Fragments; C026843:dynorphin (1-13); D004399:Dynorphins