Purification and Characterization of a Protein from Porcine Gut with Glucagon-Like Immunoreactivity

Abstract

A protein with glucagon-like immunoreactivity has been isolated from porcine intestine in a highly purified form. The isoelectric point is 6.8-6.9, and the molecular weight is 11,625, as calculated from its amino acid composition: this estimate has been confirmed by S.D.S. gel electrophoresis. The partial sequence so far elucidated is from the N-terminal: Arg-Ser-Leu-Gln-Asn-Thr-Glx-Glx-Lys-Ala-Arg-Ser-Phe-, and from the C-terminal: -lie-Ala, both differing from those of porcine pancreatic glucagon. On a molar basis the protein has the same immunoreactivity as porcine glucagon when assayed with some anti-glucagon sera, while the activity is less than 0.2% using other anti-glucagon sera.