title: 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-Gin-Asn-Thr-Glx-Glx-Lys-Ala-Arg-Ser-Phe-, and from the C-terminal: -Ile-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.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004386:Duodenum / Q000502:physiology; D005934:Glucagon / Q000276:immunology; D007082:Ileum / Q000502:physiology; D007421:Intestine, Small / Q000502:physiology*; D007583:Jejunum / Q000502:physiology; D008970:Molecular Weight; D009124:Muscle Proteins / Q000276:immunology / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D011863:Radioimmunoassay; D013552:Swine
chemical_list: D000596:Amino Acids; D009124:Muscle Proteins; D010446:Peptide Fragments; D005934:Glucagon