Isolation of glucagon‐37 (bioactive enteroglucagon/oxyntomodulin) from porcine jejuno‐ileum
D. Bataille, A M Coudray, M. Carlqvist, G Rosselin, Viktor Mutt
Abstract
D. Bataille, A M Coudray, M. Carlqvist, G Rosselin, Viktor Mutt
Abstract
A 37 amino acid-peptide has been isolated from porcine jejuno-ileum on the basis of its glucagon-like activity in liver (interaction with glucagon-binding sites and activation of adenylate cyclase) using gel filtration, ion-exchange and high-performance liquid chromatography. Depending on the criteria chosen, this peptide is referred to as either 'bioactive enteroglucagon' (activity in liver), 'oxyntomodulin' (specific action in gastric oxyntic glands) or 'glucagon-37' (chemical structure).
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A 37 amino acid-peptide has been isolated from porcine jejuno-ileum on the basis of its glucagon-like activity in liver (interaction with glucagon-binding sites and activation of adenylate cyclase) using gel filtration, ion-exchange and high-performance liquid chromatography. Depending on the criteria chosen, this peptide is referred to as either 'bioactive enteroglucagon' (activity in liver), 'oxyntomodulin' (specific action in gastric oxyntic glands) or 'glucagon-37' (chemical structure).
Key concepts: Glucagon, Ileum, Chemistry, Internal medicine, Gastrointestinal hormone, Endocrinology, Cyclase, Biochemistry