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PMID: 4525166 Published · ppublish English Journal Article

Isolation of a glucagon-containing peptide: primary structure of a possible fragment of proglucagon.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 70 ·No. 8 ·1973-08-00 ·Pages 2321-5

Tager HS, Steiner DF

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.

MeSH Terms
Amino Acid Sequence Animals Carboxypeptidases/metabolism Cattle Chromatography, Gel Chromatography, Ion Exchange Glucagon/analysis Immunoassay Molecular Weight Peptides/isolation & purification,metabolism Protein Precursors/isolation & purification Swine
Chemicals
Peptides Protein Precursors Glucagon Carboxypeptidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tager H S
Steiner D F
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.70.8.2321
Published
1973-08-00
Pages
2321-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433727
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.70.8.2321 PMC Full Text View journal details
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