Download PDF
Horm Metab Res 1976; 8(5): 366-371
DOI: 10.1055/s-0028-1093615
Originals

© Georg Thieme Verlag KG Stuttgart · New York

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

F.  Sundby , H.  Jacobsen , A. J. Moody
  • Novo Research Institute, Copenhagen, Denmark
Further Information

Publication History

Publication Date:
23 December 2008 (online)

Also available at
  PDF Download  Permissions and Reprints

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

      >