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Evidence that enteroglucagon (II) is identical with the C-terminal sequence (residues 33-69) of glicentin.

Authors
  • Holst, J J
Type
Published Article
Journal
The Biochemical journal
Publication Date
Dec 01, 1982
Volume
207
Issue
3
Pages
381–388
Identifiers
PMID: 7165698
Source
Medline
License
Unknown

Abstract

Enteroglucagon (II) was isolated from extracts of pig ileum mucosa by repeated gel filtrations, and its immunochemical and chromatographic characteristics were compared with those of a synthetic peptide corresponding to the 33-69 sequence of pig glicentin, before and after digestion with trypsin or trypsin followed by carboxypeptidase B, by using five region-specific assays covering most of the glicentin sequence. Enteroglucagon (II) and the synthetic peptide behave identically under three different conditions of chromatography as determined with all five assays (including a highly specific radioreceptor assay), and gave rise to similar fragments after enzyme digestion. It was therefore concluded that enteroglucagon (II) and the 33-69 sequence of glicentin are most probably identical.

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