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Complete amino acid sequence of a human pituitary glycopeptide: an important maturation product of pro-opiomelanocortin.
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.
PMID: 6945581 [PubMed - indexed for MEDLINE]
PMCID: PMC319764
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Cited by 4 PubMed Central articles
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Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase.
Hansen JE, Lund O, Engelbrecht J, Bohr H, Nielsen JO, Hansen JE.
Biochem J. 1995 Jun 15; 308 ( Pt 3):801-13.
[Biochem J. 1995]
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NH2-terminal amino acid sequence and peptide mapping of purified human beta-lipotropin: comparison with previously proposed sequences.
Spiess J, Mount CD, Nicholson WE, Orth DN.
Proc Natl Acad Sci U S A. 1982 Aug; 79(16):5071-5.
[Proc Natl Acad Sci U S A. 1982]
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Biosynthesis of hormonal and neural peptides.
Chrétien M, Benjannet S, Lazure C, Seidah NG.
Trans Am Clin Climatol Assoc. 1984; 95:19-25.
[Trans Am Clin Climatol Assoc. 1984]
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