Characterization of multiple forms of porcine anterior pituitary proopiomelanocortin amino-terminal glycopeptide.
Chromatography on a molecular sieve column of a preparation of porcine proopiomelanocortin N-terminal glycopeptide purified from anterior pituitary resulted in the isolation of three forms of the peptide with respective apparent Mr 21 000, 17 500, and 13 500 on polyacrylamide/sodium dodecyl sulfate gel. Determination of the amino acid composition of each peptide revealed that the form with a molecular weight of 17 500 corresponds to the 80 amino acid residue porcine N-terminal glycopeptide (PNT 1-80) previously characterized [Larivière, N., Seidah, N.G., & Chrétien, M. (1981) Int. J. Pept. Protein Res. 18, 487-491]. The forms with molecular weight of 21 000 and 13 500 correspond respectively to longer and shorter forms of the N-terminal glycopeptide. The high molecular weight form contains 107 amino acid residues. Sequencing of the fragments obtained after cleavage of the molecule with cyanogen bromide and Myxobacter Lys-C protease indicated that an extension of 27 amino acid residues is linked to PNT 1-80 through a -Lys-Arg-sequence. The sequence of the extension is reported. The low molecular weight form corresponds to the first 61 residues of PNT 1-80. Pronase digestion of the peptide and dansylation of the digest revealed the presence of a residue of phenylalanine amide at position 61. A general model for the maturation of the N-terminal glycopeptide of proopiomelanocortin in porcine anterior pituitary is presented.[1]References
- Characterization of multiple forms of porcine anterior pituitary proopiomelanocortin amino-terminal glycopeptide. Boileau, G., Larivière, N., Hsi, K.L., Seidah, N.G., Chrétien, M. Biochemistry (1982) [Pubmed]
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