Abstract
Summary
Pigeon pancreatic islets were homogenized in acid ethanol containing inhibitors of proteolysis. Purification of the extract, including fractionation on Sephadex G-50 columns, yielded a 9000-dalton protein, which after further purification by DEAE-cellulose chromatography, appeared to be homogeneous and more cati-onic than porcine glucagon on polyacryl-amide disc gel electrophoresis. When the protein obtained by DEAE-cellulose chromatography was iodinated and applied to a Sephadex G-50 column, a single radioactive peak of 9000 daltons was also obtained. The DEAE-cellulose peak is composed of 76 amino acids, including all those of turkey glucagon. Its amino acid composition is similar but not identical to that of angler fish “proglucagon”.
Get full access to this article
View all access options for this article.