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 language||English (US)|
|Number of pages||9|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Mar 31 1981|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology