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Study of frog rana esculenta proopiomelanocortin processing in the intermediate pituitary identification of alpha melanotropin beta melanotropin lys gamma melanotropin and corticotropin like intermediate lobe peptide



Study of frog rana esculenta proopiomelanocortin processing in the intermediate pituitary identification of alpha melanotropin beta melanotropin lys gamma melanotropin and corticotropin like intermediate lobe peptide



International Journal of Peptide & Protein Research 37(3): 236-240



The proteolytic processing of frog (Rana esculenta) proopiomelanocortin in melanotropic cells of the intermediate pituitary gland has been examined through purification of the mature fragments by reverse-phase high-presure liquid chromatography and microsequencing of isolated peptides. .alpha.-Melanotropin, .beta.-melanotropin, Lys-.gamma.-melanotropin, corticotropin-like intermediate lobe peptide, and hinge peptide have been isolated and chemically characterized. The results show a high preservation in the processing sites of frog proopiomelanotropin when compared to bovine counterparts. They reveal also a greater conservation of the processing enzyme equipment of melanotropic cells in tetrapods species. Identification of Lys-.gamma.-melanotropin suggests the occurrence of an endopeptidase able to cleave between two basic residues. On the other hand .alpha.-melanotropin does not appear to be N-acetylated, as previously found in the clawed-toad Xenopus laevis, and this feature might distinguish amphibian from mammalian proopiomelanocortin processing.

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Accession: 007837777

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PMID: 1651291


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