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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2002-8-6
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11996671-10224147,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
366
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
245-53
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11996671-Circular Dichroism,
pubmed-meshheading:11996671-Detergents,
pubmed-meshheading:11996671-Dimerization,
pubmed-meshheading:11996671-Dose-Response Relationship, Drug,
pubmed-meshheading:11996671-Escherichia coli,
pubmed-meshheading:11996671-Ions,
pubmed-meshheading:11996671-Kinetics,
pubmed-meshheading:11996671-Lipoproteins, HDL,
pubmed-meshheading:11996671-Phosphatidylcholines,
pubmed-meshheading:11996671-Protein Denaturation,
pubmed-meshheading:11996671-Recombinant Proteins,
pubmed-meshheading:11996671-Sodium Dodecyl Sulfate,
pubmed-meshheading:11996671-Urea
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pubmed:year |
2002
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pubmed:articleTitle |
Size is a major determinant of dissociation and denaturation behaviour of reconstituted high-density lipoproteins.
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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
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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