title: Isolation and partial characterization of anglefish proglucagon.
abstract: Evidence is presented that proglucagon from anglefish islets is a single chain polypeptide with 78 amino acid residues and that the glucagon portion of it is liberated after tryptic cleavage. The most striking characteristic in the conversion of the anglerfish proglucagon to glucagon is that the cleaved peptide bonds display enormous sensitivity toward trypsin. Thus, conversion of the prohormone to glucagon occurs very rapidly within 3-10 min with a 1:500-1:1000 molar ratio of enzyme to substrate. Further, trypic cleavage of the anglerfish glucagon requires higher concentrations of trypsin (molar ratio 1:25 enzyme to substrate) and longer incubation time. The behavior of proglucagon and glucagon toward trypsin shows striking similarities with the tryptic conversion of anglerfish proinsulin to insulin.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004589:Electrophoresis, Disc; D005399:Fishes; D005934:Glucagon / Q000302:isolation & purification; D007515:Islets of Langerhans / Q000032:analysis; D011498:Protein Precursors / Q000302:isolation & purification
chemical_list: D000596:Amino Acids; D011498:Protein Precursors; D005934:Glucagon