Abstract
Abstract The anionic detergent sodium dodecyl sulfate interacts with three to four binding sites on the surface of each of the individual polypeptide components (AI and AII) of human serum high density lipoprotein. The association constants for this process are the same for both AI and the disulfidebonded dimer of AII, namely 2 x 104 liters per mole. AI and AII are relatively compact, ordered structures over this range of detergent binding, and cooperative interaction occurs only at much higher free concentrations of ligand ( g 1.5 x 10-4 m). The detergent binding sites are probably exposed rather than clefts in the protein surface, since these same sites are involved in protein-protein interactions between the polypeptide components of high density lipoprotein.
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