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Isolation of glucagon‐37 (bioactive enteroglucagon/oxyntomodulin) from porcine jejuno‐ileum
Author(s) -
Bataille D.,
Tatemoto K.,
Gespach C.,
Jörnvall H.,
Rosselin G.,
Mutt V.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80709-6
Subject(s) - glucagon , medicine , endocrinology , chemistry , ileum , gastric inhibitory polypeptide , proglucagon , cyclase , peptide hormone , gastrointestinal hormone , biochemistry , biology , glucagon like peptide 1 , hormone , enzyme , diabetes mellitus , type 2 diabetes
A peptide isolated from porcine gut according to its glucagon‐like activity in liver (bioactive enteroglucagon) has been characterized immunologically, biologically and chemically: its potency relative to pancreatic glucagon in interacting with an antiglucagon antibody, hepatic glucagon‐binding sites and hepatic adenylate cyclase was ∼100%, 20% and 10%, respectively. In contrast, it is ∼20‐times more potent than glucagon in oxyntic glands, justifying the term ‘oxyntomodulin’. Chemically, it consists in the 29 amino acid‐peptide glucagon elongated at its C‐terminal end by the octapeptide Lys—Arg—Asn—Lys—Asn—Asn—Ile &—Ala; accordingly, it is called ‘glucagon‐37’