| pubmed-article:4048553 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C0085979 | lld:lifeskim |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C0017687 | lld:lifeskim |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C0086379 | lld:lifeskim |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C0728938 | lld:lifeskim |
| pubmed-article:4048553 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:4048553 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:4048553 | pubmed:dateCreated | 1985-11-19 | lld:pubmed |
| pubmed-article:4048553 | 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. | lld:pubmed |
| pubmed-article:4048553 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4048553 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4048553 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:4048553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4048553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4048553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4048553 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4048553 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:4048553 | pubmed:issn | 0167-0115 | lld:pubmed |
| pubmed-article:4048553 | pubmed:author | pubmed-author:ConlonJ MJM | lld:pubmed |
| pubmed-article:4048553 | pubmed:author | pubmed-author:SchwartzT WTW | lld:pubmed |
| pubmed-article:4048553 | pubmed:author | pubmed-author:HansenH FHF | lld:pubmed |
| pubmed-article:4048553 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4048553 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:4048553 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4048553 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4048553 | pubmed:pagination | 309-20 | lld:pubmed |
| pubmed-article:4048553 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:meshHeading | pubmed-meshheading:4048553-... | lld:pubmed |
| pubmed-article:4048553 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:4048553 | pubmed:articleTitle | Primary structure of glucagon and a partial sequence of oxyntomodulin (glucagon-37) from the guinea pig. | lld:pubmed |
| pubmed-article:4048553 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:4048553 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:100135526 | entrezgene:pubmed | pubmed-article:4048553 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4048553 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4048553 | lld:pubmed |
