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

Year: 1982

Type: article

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.

Source: Biochemical Journal

DOI: 10.1042/bj2070381

Author: J J Holst

Institution: University of Copenhagen

Language: English

Topic: Neuropeptides and Animal Physiology

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

Open Access status: bronze

Funders: Sundhed og Sygdom, Det Frie Forskningsråd, Medical Research Council

OpenAlex ID: W2283885169