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- W1538963458 abstract "The results indicate that (a) apo-A-II can generate HDL complexes, although these are heterogeneous in size and density; (b) the formation of these complexes requires well defined conditions, particularly with regard to initial protein concentration and lipid/protein ratio; (c) below and above the optimal apo-A-II concentration for HDL reassembly, reassociation of apo-A-II with lipids is minimal, probably due to changes in conformation or state of association, or both, of the apoprotein; and (d) at lipid/apo-A-II ratios above 1, the formation of lipid-rich particles is due to a process characterized by an adsorption of apo-A-II to thermodynamically stable lipid vesicles followed by their disruption into particles heterogeneous in size and density. We conclude that the interaction of apo-A-II with HDL lipids is extremely sensitive to experimental conditions and that apo-A-II can be incorporated into lipoprotein particles of much broader distribution than those previously obtained in similar reassembly studies involving apolipoprotein A-I." @default.
- W1538963458 created "2016-06-24" @default.
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- W1538963458 date "1979-04-10" @default.
- W1538963458 modified "2023-09-27" @default.
- W1538963458 title "Apolipoprotein A-II and structure of human serum high density lipoproteins" @default.
- W1538963458 hasPublicationYear "1979" @default.
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