| pubmed-article:3542510 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C1415067 | lld:lifeskim |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C0470187 | lld:lifeskim |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C1521827 | lld:lifeskim |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C2700400 | lld:lifeskim |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:3542510 | lifeskim:mentions | umls-concept:C0205254 | lld:lifeskim |
| pubmed-article:3542510 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3542510 | pubmed:dateCreated | 1987-3-4 | lld:pubmed |
| pubmed-article:3542510 | pubmed:abstractText | Commercially available preparations of natural porcine glucose-dependent insulinotropic polypeptide (GIP) were subjected to reverse phase HPLC. The material was found to give rise to 4 peaks which were characterized by HPLC-retention time and N-terminal sequence analysis. They represented: intact porcine GIP(1-42), 58% (wt/wt); the GIP-fragment des-tyr-ala-GIP(3-42), 32% (wt/wt); cholecystokinin (CCK)-33 2% (wt/wt); CCK-39 2% (wt/wt). HPLC-pure GIP(1-42) stimulated insulin release in rat isolated pre-cultured pancreatic islets in the presence of 16.7 mM glucose up to 240% vs. control, whereas the fragment des-tyr-ala-GIP(3-42) did neither increase insulin release nor exhibit antagonistic activity to GIP(1-42) at 100 ng/ml. These results indicate that commercially available porcine GIP-preparations may contain the biologically inactive des-tyr-ala-GIP(3-42) in high amounts, and in addition may be contaminated by CCK-peptides. HPLC-characterization of these peptide preparations prior to any biological study is crucial. | lld:pubmed |
| pubmed-article:3542510 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3542510 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:3542510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3542510 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3542510 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:3542510 | pubmed:issn | 0013-7227 | lld:pubmed |
| pubmed-article:3542510 | pubmed:author | pubmed-author:CreutzfeldtWW | lld:pubmed |
| pubmed-article:3542510 | pubmed:author | pubmed-author:SchmidtW EWE | lld:pubmed |
| pubmed-article:3542510 | pubmed:author | pubmed-author:SiegelE GEG | lld:pubmed |
| pubmed-article:3542510 | pubmed:author | pubmed-author:KümmelHH | lld:pubmed |
| pubmed-article:3542510 | pubmed:author | pubmed-author:GallwitzBB | lld:pubmed |
| pubmed-article:3542510 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3542510 | pubmed:volume | 120 | lld:pubmed |
| pubmed-article:3542510 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3542510 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3542510 | pubmed:pagination | 835-7 | lld:pubmed |
| pubmed-article:3542510 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:meshHeading | pubmed-meshheading:3542510-... | lld:pubmed |
| pubmed-article:3542510 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3542510 | pubmed:articleTitle | Commercially available preparations of porcine glucose-dependent insulinotropic polypeptide (GIP) contain a biologically inactive GIP-fragment and cholecystokinin-33/-39. | lld:pubmed |
| pubmed-article:3542510 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3542510 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3542510 | lld:pubmed |
