Reconstituted high-density lipoproteins with a disulfide-linked apolipoprotein A-I dimer: evidence for restricted particle size heterogeneity

The lipid-binding properties of apolipopotein recombinant homodimer (A-I(sub M)/A-I(sub M)) and normal apolipoprotein (apoA-I) were comparatively studied. The dimerization of apoA-I did not affect the rate off association of apoA-I with phospholipids. The introduction of an interchain disulfide bridge in apoA-I limited the high-density lipoprotein heterogeneity. A-I(sub M)/A-I(sub M) behaved as a stable form of apoA-I.