Studies on human serum high-density lipoproteins. Self-association of human serum apolipoprotein A-II in aqueous solutions.
Some of the solution properties of pure preparations of human serum high-density apolipoprotein A-II were studied by sedimentation equilibrium ultracentrifugation, conducted at different apoprotein concentrations and at several speeds. The concentration dependence of the apparent weight average molecular weight indicated that apolipoprotein A-II, when dissolved in 0.02 MEDTA (pH 8.6), undergoes self-association. Over a protein concentration range between 0.8 and 1.5 mg/ml, the self-association could best be described by a monomer-dimer-trimer step association, although indefinite self-association could not be ruled out. The equilibrium constants obtained were sufficient to describe the system over the concentration range investigated.
D001665:Binding Sites; D006801:Humans; D008075:Lipoproteins, HDL / Q000097:blood*; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D011487:Protein Conformation; D014461:Ultracentrifugation
D008075:Lipoproteins, HDL; D046911:Macromolecular Substances