Effect of pressure and ionic strength on the self-association of Apo-A-I from the human high density lipoprotein complex.
The self-association of apo-A-I isolated from the human high density lipoprotein complex has been investigated by gel permeation chromatography and sedimentation equilibrium. The apparent weight average molecular weight (MWapp) versus Apo-A-I concentration profile was found to be sensitive to ionic strength and pressure; MWapp increased with increasing ionic strength and decreasing rotor speed. The data were consistent with a monomer-dimer-tetrameroctamer association shceme over all conditions investigated if a change in the partial specific volume of apo-A-I upon association of 5.5 x 10(-2) ml/g is postulated.
D001053:Apolipoproteins / Q000097:blood; D006801:Humans; D007700:Kinetics; D008075:Lipoproteins, HDL / Q000097:blood; D046911:Macromolecular Substances; D009994:Osmolar Concentration; D011312:Pressure; D011487:Protein Conformation; D013816:Thermodynamics
D001053:Apolipoproteins; D008075:Lipoproteins, HDL; D046911:Macromolecular Substances