Isolation of alpha-melanotropin and N, O-diacetylserine1-alpha-melanotropin from porcine pituitary extracts.
In the course of isolation of alpha-melanotropin (alpha-MSH) from porcine pituitary extracts, a peptide with identical amino acid composition but slightly less polar properties compared to alpha-MSH was detected and isolated by partition chromatography. The new peptide was identified as N, O-diacetyl-Ser1-alpha-MSH by high resolution nuclear magnetic resonance spectroscopy. N, O-diacetyl-Ser1-alpha-MSH was readily converted to alpha-MSH by incubation at pH 9.5. The O-acetyl analog of alpha-MSH was found to be as active as alpha-MSH in stimulating lipolysis in isolated rabbit adipocytes.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D009074:Melanocyte-Stimulating Hormones / Q000302:isolation & purification*; D010902:Pituitary Gland / Q000098:blood supply*; D011817:Rabbits; D013552:Swine
D000596:Amino Acids; D009074:Melanocyte-Stimulating Hormones