title: Evidence that glicentin contains the entire sequence of glucagon.
abstract: Glicentin (a highly purified 100-amino acid peptide with glucagon-like immunoreactivity from porcine gut) was subjected to limited digestion with trypsin and carboxypeptidase B, and the resulting peptides were studied by gel filtration and region-specific glucagon radioimmunoassays. Similar digests of glucagon and purified fragments of glucagon were studied in parallel. Glicentin gave rise to peptides that corresponded closely to the 1-17 and 19-29 fragments of glucagon. Also, 125I-labelled glicentin and 125I-labelled glucagon gave rise to identical fragments after trypsin treatment. On the basis of this and other evidence [Jacobsen, Demandt, Moody & Sundby (1977) Biochim. Biophys. Acta 493, 452-459] it is concluded that glicentin contains the entire glucagon sequence at residues number 64-92 and thus fulfills one of the requirements for being a 'proglucagon'.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D005934:Glucagon / Q000032:analysis*; D004763:Glucagon-Like Peptides; D007106:Immune Sera; D010455:Peptides / Q000276:immunology; D013552:Swine; D014357:Trypsin
chemical_list: D007106:Immune Sera; D010455:Peptides; D004763:Glucagon-Like Peptides; C015236:glucagon-like-immunoreactivity; D005934:Glucagon; D014357:Trypsin