Human plasma high density apolipoprotein A-I: Effect of protein-protein interactions on the spontaneous formation of a lipid-protein recombinant

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Abstract

The effect of the self-association of apolipoprotein A-I on the dynamics of lipid-protein complex formation was studied. Treatment of self-associated apolipoprotein A-I with guanidine hydrochloride initially resulted in dissociation of the oligomers into monomers and subsequent denaturation of the monomers. The association of monomeric and oligomeric apolipoprotein A-I with dimyristoylphosphatidylcholine resulted in identical lipid-protein recombinants as determined by chemical analysis and gel-filtration column elution profiles. Denaturation of a recombinant with guanidine hydrochloride indicated that the protein is more stable in a lipid-protein recombinant than as an oligomer; however, self-association does decrease the rate of lipidprotein recombinant formation. Because apolipoprotein A-I is more stable when it is associated with lipid, we conclude that the association of this protein with a variety of lipids is subject to kinetic control.

Original languageEnglish (US)
Pages (from-to)466-474
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume99
Issue number2
DOIs
StatePublished - Mar 31 1981

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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