Further Characterization of a Glucagon Precursor from Anglerfish Islet Tissue

Abstract
Summary Anglerfish proglucagon, isolated by gel filtration, was found to be stable in 8 M urea and to resist ribonuclease treatment, indicating its monomeric form and absence of ribonucleic acid moieties. Cleavage products of chymotrypsin-treated or trypsin-treated proglucagon are similar in molecular size. The migration pattern of anglerfish proglucagon on polyacrylamide gels (pH 8.3) indicates that the molecule is more electronegative than glucagon. The approximate molecular weight of anglerfish proglucagon is 11,400 ± 400 daltons.