| pubmed-article:11996671 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11996671 | lifeskim:mentions | umls-concept:C0023821 | lld:lifeskim |
| pubmed-article:11996671 | lifeskim:mentions | umls-concept:C0004927 | lld:lifeskim |
| pubmed-article:11996671 | lifeskim:mentions | umls-concept:C0086168 | lld:lifeskim |
| pubmed-article:11996671 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:11996671 | lifeskim:mentions | umls-concept:C0456389 | lld:lifeskim |
| pubmed-article:11996671 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:11996671 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:11996671 | pubmed:dateCreated | 2002-8-6 | lld:pubmed |
| pubmed-article:11996671 | pubmed:abstractText | Lipid-free apolipoprotein A-I (apoA-I) and A-I(Milano) (A-I(M)) were compared for their denaturation behaviour by running across transverse gradients of a chaotrope, urea, and of a ionic detergent, SDS. For both apo A-I and monomeric apoA-I(M) in the presence of increasing concentrations of urea the transition from high to low mobility had a sigmoidal course, whereas for dimeric A-I(M)/A-I(M) a non-sigmoidal shape was observed. The co-operativity of the unfolding process was lower for dimeric A-I(M)/A-I(M) than for apoA-I or for monomeric apoA-I(M). A slightly higher susceptibility to denaturation was observed for dimeric A-I(M)/A-I(M) than for monomeric apoA-I(M). A similar behaviour of A-I(M)/A-IM versus apoA-I(M) was observed in CD experiments. Large- (12.7/12.5 nm) and small- (7.8 nm) sized reconstituted high-density lipoproteins (rHDL) containing either apoA-I or A-I(M)/A-I(M) were compared with respect to their protein-lipid dissociation behaviour by subjecting them to electrophoresis in the presence of urea, of SDS and of a non-ionic detergent, Nonidet P40. A higher susceptibility to dissociation of small-sized versus large-sized rHDL, regardless of the apolipoprotein component, was observed in all three instances. Our data demonstrate that the differential plasticity of the various classes of rHDL is a function of their size; the higher stability of 12.5/12.7 nm rHDL is likely connected to the higher number of protein-lipid and lipid-lipid interactions in larger as compared with smaller rHDL. | lld:pubmed |
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| pubmed-article:11996671 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11996671 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11996671 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11996671 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11996671 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11996671 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11996671 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11996671 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:11996671 | pubmed:author | pubmed-author:CalabresiLaur... | lld:pubmed |
| pubmed-article:11996671 | pubmed:author | pubmed-author:FranceschiniG... | lld:pubmed |
| pubmed-article:11996671 | pubmed:author | pubmed-author:SirtoriCesare... | lld:pubmed |
| pubmed-article:11996671 | pubmed:author | pubmed-author:EberiniIvanoI | lld:pubmed |
| pubmed-article:11996671 | pubmed:author | pubmed-author:GianazzaElisa... | lld:pubmed |
| pubmed-article:11996671 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11996671 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11996671 | pubmed:volume | 366 | lld:pubmed |
| pubmed-article:11996671 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11996671 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11996671 | pubmed:pagination | 245-53 | lld:pubmed |
| pubmed-article:11996671 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11996671 | pubmed:meshHeading | pubmed-meshheading:11996671... | lld:pubmed |
| pubmed-article:11996671 | pubmed:meshHeading | pubmed-meshheading:11996671... | lld:pubmed |
| pubmed-article:11996671 | pubmed:meshHeading | pubmed-meshheading:11996671... | lld:pubmed |
| pubmed-article:11996671 | pubmed:meshHeading | pubmed-meshheading:11996671... | lld:pubmed |
| pubmed-article:11996671 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11996671 | pubmed:articleTitle | Size is a major determinant of dissociation and denaturation behaviour of reconstituted high-density lipoproteins. | lld:pubmed |
| pubmed-article:11996671 | pubmed:affiliation | Gruppo di Studio per la Proteomica e la Struttura delle Proteine, Dipartimento di Scienze Farmacologiche, Università degli Studi di Milano, via G. Balzaretti 9, I-20133 Milano, Italy. elisabetta.gianazza@unimi.it | lld:pubmed |
| pubmed-article:11996671 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11996671 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11996671 | lld:pubmed |
