Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:16682228rdf:typepubmed:Citationlld:pubmed
pubmed-article:16682228lifeskim:mentionsumls-concept:C0914069lld:lifeskim
pubmed-article:16682228lifeskim:mentionsumls-concept:C0017262lld:lifeskim
pubmed-article:16682228lifeskim:mentionsumls-concept:C2911684lld:lifeskim
pubmed-article:16682228lifeskim:mentionsumls-concept:C0185117lld:lifeskim
pubmed-article:16682228pubmed:issue2lld:pubmed
pubmed-article:16682228pubmed:dateCreated2006-7-28lld:pubmed
pubmed-article:16682228pubmed:abstractTextLipoprotein-associated phospholipase A(2) (Lp-PLA(2)) is a key enzyme involved in atherosclerosis, and has been considered as a new target for drug discovery. The major difficulty for high-throughput screening of Lp-PLA(2) inhibitors and for functional studies was their fast and efficient production. Purification of native Lp-PLA(2) from human plasma was complicated and produced a very low yield. We herein examined the feasibility of expressing and purifying recombinant Lp-PLA(2) in different heterologous expression systems. The fusion Lp-PLA(2) was expressed at high levels and exhibited strong enzyme activity in insect cell-baculovirus expression system. The functional enzyme could also be produced in Pichia pastoris. The inclusion of a Kozak sequence increased greatly the expression level of recombinant Lp-PLA(2) in insect cells, but had little effect on the expression of recombinant Lp-PLA(2) in P. pastoris and Escherichia coli. P. pastoris-produced Lp-PLA(2) could be purified rapidly and conveniently through a one-step procedure, while baculovirus-produced Lp-PLA(2) could be efficiently purified through a two-step procedure. This ability to readily produce recombinant Lp-PLA(2) could provide a screening model for Lp-PLA(2) inhibitors and will facilitate further studies on this enzyme.lld:pubmed
pubmed-article:16682228pubmed:languageenglld:pubmed
pubmed-article:16682228pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16682228pubmed:citationSubsetIMlld:pubmed
pubmed-article:16682228pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16682228pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16682228pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16682228pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:16682228pubmed:statusMEDLINElld:pubmed
pubmed-article:16682228pubmed:monthAuglld:pubmed
pubmed-article:16682228pubmed:issn1046-5928lld:pubmed
pubmed-article:16682228pubmed:authorpubmed-author:WangYipingYlld:pubmed
pubmed-article:16682228pubmed:authorpubmed-author:DongLiLlld:pubmed
pubmed-article:16682228pubmed:authorpubmed-author:ShenJingkangJlld:pubmed
pubmed-article:16682228pubmed:authorpubmed-author:ZhangFujunFlld:pubmed
pubmed-article:16682228pubmed:authorpubmed-author:CaiMaojunMlld:pubmed
pubmed-article:16682228pubmed:issnTypePrintlld:pubmed
pubmed-article:16682228pubmed:volume48lld:pubmed
pubmed-article:16682228pubmed:ownerNLMlld:pubmed
pubmed-article:16682228pubmed:authorsCompleteYlld:pubmed
pubmed-article:16682228pubmed:pagination300-6lld:pubmed
pubmed-article:16682228pubmed:dateRevised2007-11-15lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:meshHeadingpubmed-meshheading:16682228...lld:pubmed
pubmed-article:16682228pubmed:year2006lld:pubmed
pubmed-article:16682228pubmed:articleTitleHeterologous expression of lipoprotein-associated phospholipase A2 in different expression systems.lld:pubmed
pubmed-article:16682228pubmed:affiliationState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, China.lld:pubmed
pubmed-article:16682228pubmed:publicationTypeJournal Articlelld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:16682228lld:pubmed