Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:7601162rdf:typepubmed:Citationlld:pubmed
pubmed-article:7601162lifeskim:mentionsumls-concept:C0039005lld:lifeskim
pubmed-article:7601162lifeskim:mentionsumls-concept:C0040165lld:lifeskim
pubmed-article:7601162lifeskim:mentionsumls-concept:C0006556lld:lifeskim
pubmed-article:7601162lifeskim:mentionsumls-concept:C0032923lld:lifeskim
pubmed-article:7601162lifeskim:mentionsumls-concept:C1167622lld:lifeskim
pubmed-article:7601162lifeskim:mentionsumls-concept:C0678594lld:lifeskim
pubmed-article:7601162lifeskim:mentionsumls-concept:C0871161lld:lifeskim
pubmed-article:7601162pubmed:issue3lld:pubmed
pubmed-article:7601162pubmed:dateCreated1995-8-10lld:pubmed
pubmed-article:7601162pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:abstractTextThyroxine binding to proteins in pig plasma during electrophoresis was observed in the albumin, but not in the prealbumin and post-albumin regions. Transthyretin could be identified in medium from in vitro pig choroid plexus incubations by size and number of subunits and a very high rate of synthesis and secretion. Its electrophoretic mobility was intermediate between that of thyroxine-binding globulin and albumin. It bound thyroxine, retinol-binding protein, anti-(rat transthyretin) antibodies and behaved similarly to transthyretins from other vertebrate species when plasma was extracted with phenol. Inhibition experiments with the synthetic flavonoid F 21388, analysing the binding of thyroxine, suggested that transthyretin is not a major thyroxine carrier in the bloodstream of pigs. Cloning and sequencing of transthyretin cDNA from both choroid plexus and liver showed that the same transthyretin mRNA is expressed in pig choroid plexus and liver. The amino acid sequence derived from the nucleotide sequence revealed that pig transthyretin differs from the transthyretins of all other studied vertebrate species by an unusual C-terminal extension consisting of the amino acids glycine, alanine and leucine. This extension results from the mutation of a stop codon into a codon for glycine. The unusual C-terminal extensions do not seem to interfere with the access of thyroxine to its binding site in the central channel of transthyretin.lld:pubmed
pubmed-article:7601162pubmed:languageenglld:pubmed
pubmed-article:7601162pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:citationSubsetIMlld:pubmed
pubmed-article:7601162pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7601162pubmed:statusMEDLINElld:pubmed
pubmed-article:7601162pubmed:monthJunlld:pubmed
pubmed-article:7601162pubmed:issn0014-2956lld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:SchreiberGGlld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:KöhrleJJlld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:ChangLLlld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:HamilE MEMlld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:RichardsonS...lld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:SouthwellB...lld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:BrackC MCMlld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:DuanWWlld:pubmed
pubmed-article:7601162pubmed:authorpubmed-author:PetterssonT...lld:pubmed
pubmed-article:7601162pubmed:issnTypePrintlld:pubmed
pubmed-article:7601162pubmed:day15lld:pubmed
pubmed-article:7601162pubmed:volume230lld:pubmed
pubmed-article:7601162pubmed:ownerNLMlld:pubmed
pubmed-article:7601162pubmed:authorsCompleteYlld:pubmed
pubmed-article:7601162pubmed:pagination977-86lld:pubmed
pubmed-article:7601162pubmed:dateRevised2007-7-23lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:meshHeadingpubmed-meshheading:7601162-...lld:pubmed
pubmed-article:7601162pubmed:year1995lld:pubmed
pubmed-article:7601162pubmed:articleTitleBinding of thyroxine to pig transthyretin, its cDNA structure, and other properties.lld:pubmed
pubmed-article:7601162pubmed:affiliationRussell Grimwade School of Biochemistry, University of Melbourne, Australia.lld:pubmed
pubmed-article:7601162pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7601162pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:397419entrezgene:pubmedpubmed-article:7601162lld:entrezgene