Evidence that enteroglucagon (II) is identical with the C-terminal sequence (residues 33-69) of glicentin.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D005768:Gastrointestinal Hormones / Q000302:isolation & purification; D005934:Glucagon; D004763:Glucagon-Like Peptides / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D052336:Proglucagon; D011498:Protein Precursors; D013552:Swine
D005768:Gastrointestinal Hormones; D010446:Peptide Fragments; D011498:Protein Precursors; D052336:Proglucagon; D004763:Glucagon-Like Peptides; D005934:Glucagon