Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9022284rdf:typepubmed:Citationlld:pubmed
pubmed-article:9022284lifeskim:mentionsumls-concept:C0020792lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C1135183lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C0013935lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C0204727lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C0205409lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C0332255lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C0178499lld:lifeskim
pubmed-article:9022284lifeskim:mentionsumls-concept:C1527178lld:lifeskim
pubmed-article:9022284pubmed:issue11lld:pubmed
pubmed-article:9022284pubmed:dateCreated1997-3-28lld:pubmed
pubmed-article:9022284pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:databankReferencehttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:abstractTextBetween days 11 and 12 of gestation, the porcine conceptus undergoes a metamorphosis from a spherical blastocyst to an elongate thread-like form. During this process, the conceptus secretes a variety of products. One of these products is protein previously referred to as porcine embryonic basic protein (BP). This protein has been shown to be a major secreted product between days 13 and 18. In this study, we report a simple two-step procedure to isolate BP from day 15 porcine conceptus conditioned medium, utilized ion-exchange chromatography and reverse-phase HPLC. Purified BP was subjected to Edman degradation amino-terminal sequencing and a 25 amino acid residue sequence was obtained. Comparing the N-terminal sequence of BP to sequences in the GenBank database determined that BP shared amino acid homology with porcine pregnancy-associated glycoprotein-2 (PAG-2). The region of identity corresponded to an internal site of PAG-2, suggesting BP was a proteolytic fragment of PAG-2. The purified protein was confirmed to be BP by Western blot using a previously characterized anti-BP antiserum. Also, the BP was immunolocalized with the trophectoderm of day 11 blastocysts. Staining intensity was diminished in spherical blastocysts compared to elongated blastocysts. Although the function of PAG-2 and its cleavage product BP are unknown, the large quantity produced by the porcine conceptus and its sequence conservation across species may indicate a necessary role in early pregnancy.lld:pubmed
pubmed-article:9022284pubmed:languageenglld:pubmed
pubmed-article:9022284pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:citationSubsetIMlld:pubmed
pubmed-article:9022284pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9022284pubmed:statusMEDLINElld:pubmed
pubmed-article:9022284pubmed:monthNovlld:pubmed
pubmed-article:9022284pubmed:issn1357-2725lld:pubmed
pubmed-article:9022284pubmed:authorpubmed-author:GodkinJ DJDlld:pubmed
pubmed-article:9022284pubmed:authorpubmed-author:BíroVVlld:pubmed
pubmed-article:9022284pubmed:authorpubmed-author:KatteshH GHGlld:pubmed
pubmed-article:9022284pubmed:issnTypePrintlld:pubmed
pubmed-article:9022284pubmed:volume28lld:pubmed
pubmed-article:9022284pubmed:ownerNLMlld:pubmed
pubmed-article:9022284pubmed:authorsCompleteYlld:pubmed
pubmed-article:9022284pubmed:pagination1249-55lld:pubmed
pubmed-article:9022284pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:meshHeadingpubmed-meshheading:9022284-...lld:pubmed
pubmed-article:9022284pubmed:year1996lld:pubmed
pubmed-article:9022284pubmed:articleTitleIsolation and identification of porcine embryonic basic protein as a fragment of pregnancy-associated glycoprotein-2.lld:pubmed
pubmed-article:9022284pubmed:affiliationDepartment of Animal Science, University of Tennessee, Knoxville 37901, USA.lld:pubmed
pubmed-article:9022284pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9022284pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed