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DOI: 10.1055/s-0028-1093615
© Georg Thieme Verlag KG Stuttgart · New York
Purification and Characterization of a Protein from Porcine Gut with Glucagon-Like Immunoreactivity
Publication History
Publication Date:
23 December 2008 (online)
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.
Key words
Porcine Gut - Glucagon-like Immunoreactivity - Purification - Characterization