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. 1973 Aug;70(8):2321–2325. doi: 10.1073/pnas.70.8.2321

Isolation of a Glucagon-containing Peptide: Primary Structure of a Possible Fragment of Proglucagon

Howard S Tager 1, Donald F Steiner 1
PMCID: PMC433727  PMID: 4525166

Abstract

The heterogeneity of crystalline bovine (ox)/porcine glucagon has been examined by gel filtration and ion-exchange chromatography. A strongly basic peptide that reacted well with antibodies to bovine/porcine glucagon was isolated and its primary structure was determined. The amino-acid sequence of the NH2-terminal 29 residues of the 4500-dalton peptide is identical with that of intact bovine or porcine glucagon. The remaining eight residues at its COOH-terminus are Lys-Arg-Asn-Asn-Lys-Asn-Ile-Ala. Small amounts of other glucagon-immunoreactive peptides having molecular weights ranging from 3700 to 9000 were also detected in crystals of bovine/porcine glucagon. We propose that the 37-residue peptide is a fragment of bovine or porcine proglucagon.

Keywords: hormones, precursors

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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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