Particular processing of pro-opiomelanocortin in Xenopus laevis intermediate pituitary. Sequencing of alpha- and beta-melanocyte-stimulating hormones.
alpha- and beta-melanocyte-stimulating hormones (alpha-MSH and beta-MSH) have been isolated from Xenopus laevis neurointermediate pituitary and microsequenced. Intracellular alpha-MSH is not N-acetylated after proteolytic processing of pro-opiomelanocortin in contrast to mammalian alpha-MSHs. There is a high preservation of the melanotropic amino acid sequence common to all MSHs although in Xenopus beta-MSH a histidine residue replaces the glutamic acid residue found in position 8 of mammalian beta-MSHs.
Rouillé
Y
Y
Laboratory of Biological Chemistry, University of Paris VI, France.
Michel
G
G
Chauvet
M T
MT
Chauvet
J
J
Acher
R
R
D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005971:Glutamates; D018698:Glutamic Acid; D006639:Histidine; D009074:Melanocyte-Stimulating Hormones / Q000032:analysis* / Q000378:metabolism; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism; D010902:Pituitary Gland / Q000032:analysis* / Q000378:metabolism; D011333:Pro-Opiomelanocortin / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D014982:Xenopus laevis / Q000378:metabolism*; D000521:alpha-MSH / Q000032:analysis* / Q000378:metabolism
D005971:Glutamates; D018698:Glutamic Acid; D006639:Histidine; D000521:alpha-MSH; D011333:Pro-Opiomelanocortin; D009074:Melanocyte-Stimulating Hormones; D010447:Peptide Hydrolases