| pubmed-article:7957205 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:7957205 | lifeskim:mentions | umls-concept:C1431573 | lld:lifeskim |
| pubmed-article:7957205 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7957205 | pubmed:dateCreated | 1994-12-21 | lld:pubmed |
| pubmed-article:7957205 | pubmed:abstractText | We have expressed recombinant human apolipoprotein A-II (apoA-II) in Escherichia coli, as a fusion protein with Schistosoma japonicum glutathione-S-transferase (GST). The GST-AII fusion protein was recovered by affinity chromatography using glutathione as a ligand. After thrombin cleavage and removal of the GST carrier, recombinant apoA-II was obtained in a highly purified form and was exclusively composed of dimeric apoA-II. Kinetics of association to dimyristoylglycerophosphocholine (Myr2GroPCho) vesicles showed that recombinant apoA-II exhibited the same pattern of association as human plasma apoA-II. Electron microscopic analysis of the complexes showed a typical pattern of rouleaux, characteristic of stacked discs, with a diameter similar to that determined by gradient-gel electrophoresis. Circular dichroism measurements showed that the alpha-helical content of both plasma and recombinant apoA-II increased similarly when the proteins associated with Myr2GroPCho vesicles, at the expense of a random-coil structure. Lipid-bound apoA-II consisted of 70-72% alpha helices, suggesting the presence of three 18-residue alpha helices/apoA-II monomer. Cross-linking experiments indicated that Myr2GroPCho complexes contained two molecules dimeric apoA-II/vesicle. Recombinant apoA-II was as efficient as plasma apoA-II in associating with HDL subclasses, and in displacing apoA-I from dipalmitoylglycerophosphocholine/cholesterol/apoA-I complexes, most likely due to its highly ordered secondary structure when associated with Myr2GroPCho vesicles. These findings demonstrate that recombinant apoA-II exhibits the same structural and functional properties as human plasma apoA-II. Thus, the expression system utilized is appropriate to produce mutagenized forms to further structure/function analysis. | lld:pubmed |
| pubmed-article:7957205 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7957205 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7957205 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7957205 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7957205 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:JungGG | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:RosseneuMM | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:LopezJJ | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:ChambazJJ | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:VanlooBB | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:ColletXX | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:LattaMM | lld:pubmed |
| pubmed-article:7957205 | pubmed:author | pubmed-author:DeneflePP | lld:pubmed |
| pubmed-article:7957205 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7957205 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7957205 | pubmed:volume | 225 | lld:pubmed |
| pubmed-article:7957205 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7957205 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7957205 | pubmed:pagination | 1141-50 | lld:pubmed |
| pubmed-article:7957205 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
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| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:meshHeading | pubmed-meshheading:7957205-... | lld:pubmed |
| pubmed-article:7957205 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7957205 | pubmed:articleTitle | Purification and characterization of recombinant human apolipoprotein A-II expressed in Escherichia coli. | lld:pubmed |
| pubmed-article:7957205 | pubmed:affiliation | URA CNRS 1283, Institut des Cordeliers, Paris, France. | lld:pubmed |
| pubmed-article:7957205 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7957205 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7957205 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
