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

Overview

MeSH Major

  • Obesity
  • Thinness
  • Weight Gain

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. © 1981.

publication date

  • March 31, 1981

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0006-291X(81)91768-X

PubMed ID

  • 6786293

Additional Document Info

start page

  • 466

end page

  • 74

volume

  • 99

number

  • 2