Linked Life Data

4048553

Source:http://linkedlifedata.com/resource/pubmed/id/4048553

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1985-11-19
pubmed:abstractText
Two glucagon-like peptides have been isolated from guinea pig pancreas and their primary structures determined. A 29-residue peptide is identical to the glucagons from all other mammals yet studied in the N-terminal region (residues 1-20) but the C-terminal region [Gln-Phe-Leu-Lys-Trp-Leu-Leu-Asn-Val] contains five substitutions. A 37-residue peptide probably represents guinea pig glucagon extended from the C-terminus by [Lys-Arg-Asn-Arg-Asn-Asn-Ile-Ala] and is analogous to human oxyntomodulin (glucagon-37). The structures suggest evolutionary pressure to conserve the N-terminal region of glucagon and the C-terminal region of oxyntomodulin. The biological activity of guinea pig glucagon has not yet been determined but it is speculated that changes in the C-terminal region of glucagon may have produced a molecule with reduced biological potency that is appropriate to the reduced potency of guinea pig insulin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0167-0115
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
309-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Primary structure of glucagon and a partial sequence of oxyntomodulin (glucagon-37) from the guinea pig.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't