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

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1973 Aug 1

PMID 4525166

Citations 34

Authors

H S Tager

D F Steiner

Affiliations

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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 NH(2)-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.

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