Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Amino Acid Sequence
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Animals
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Chromatography, High Pressure Liquid
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Glutamates
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Glutamic Acid
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Histidine
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Melanocyte-Stimulating Hormones / analysis*
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Melanocyte-Stimulating Hormones / metabolism
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Molecular Sequence Data
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Peptide Hydrolases / metabolism
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Pituitary Gland / analysis*
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Pituitary Gland / metabolism
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Pro-Opiomelanocortin / metabolism*
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Sequence Homology, Nucleic Acid
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Xenopus laevis / metabolism*
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alpha-MSH / analysis*
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alpha-MSH / metabolism
Substances
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Glutamates
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Glutamic Acid
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Histidine
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alpha-MSH
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Pro-Opiomelanocortin
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Melanocyte-Stimulating Hormones
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Peptide Hydrolases