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  • Title: Purification and characterization of a protein from porcine gut with glucagon-like immunoreactivity.
    Author: Sundby F, Jacobsen H, Moody AJ.
    Journal: Horm Metab Res; 1976 Sep; 8(5):366-71. PubMed ID: 976935.
    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.
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