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. 1981 Jul;78(7):4236–4240. doi: 10.1073/pnas.78.7.4236

Complete amino acid sequence of a human pituitary glycopeptide: an important maturation product of pro-opiomelanocortin.

N G Seidah, M Chrétien
PMCID: PMC319764  PMID: 6945581

Abstract

A glycopeptide isolated in relatively large amounts from human pituitary glands was completely purified, and its sequence was determined. The primary sequence represents the NH2-terminal 76 amino acid residues of pro-opiomelanocortin (POMC). This important secretory product of POMC was shown to possess an interesting aldosterone-stimulating activity on a human adrenal aldosteronoma. It is O-glycosylated at Thr-45 and N-glycosylated at Asn-65. Only one sequence variation with the human genomic DNA was found. Furthermore, comparison with the other preferred cleavage sites of human POMC reveals that the pair of basic residues Lys-Arg represents the major sites of enzymatic maturation of this precursor molecule. This predicts a highly specific type of enzyme involved in the maturation of POMC in the anterior lobe of the human pituitary.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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