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2. Effect of pressure and ionic strength on the self-association of Apo-A-I from the human high density lipoprotein complex

Author

J C Osborne, H B Brewer, S Formisano, Formisano, Silvestro, Brewer H. B., Jr, and Osborne, J. C. J. r.

Subjects
Chemistry, Kinetics, Analytical chemistry, Cell Biology, Biochemistry, Osmolar Concentration, Gel permeation chromatography, chemistry.chemical_compound, High-density lipoprotein, Partial specific volume, Ionic strength, Sedimentation equilibrium, Molar mass distribution, Molecular Biology
Abstract

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.

Published
1978

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