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pubmed-article:3964275pubmed:abstractTextWe have studied the lipoprotein distribution of human apo A-IV during cholesterol esterification by the action of endogenous lecithin-cholesterol acyltransferase. Using immunologic and radiotracer techniques at 4 degrees C, apo A-IV was found in two discrete monomeric and dimeric populations, unassociated with plasma lipoproteins. With incubation at 37 degrees C, apo A-IV initially associated with the high density lipoprotein-3 fraction, but thereafter dissociated from its surface, and reappeared as unbound protein and in association with a complex in the low density lipoprotein size range. Inclusion of LCAT inhibitors in the incubations abolished these changes. We conclude that the changes in lipoprotein distribution of human apo A-IV closely parallel the formation and exchange of plasma cholesteryl esters.lld:pubmed
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pubmed-article:3964275pubmed:authorpubmed-author:WeinbergR BRBlld:pubmed
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pubmed-article:3964275pubmed:pagination756-63lld:pubmed
pubmed-article:3964275pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:3964275pubmed:year1986lld:pubmed
pubmed-article:3964275pubmed:articleTitleLipoprotein affinity of human apolipoprotein A-IV during cholesterol esterification.lld:pubmed
pubmed-article:3964275pubmed:publicationTypeJournal Articlelld:pubmed
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