Size and Shape Determination of Native and Defatted Bovine Serum Albumin Monomers

II. Influence of the Fatty Acid Content on the Conformation of Bovine Serum Albumin Monomers

抄録

The fatty acid content of bovine serum albumin (BSA) monomer samples was altered either through delipidation or relipidation with long-chain fatty acids. The investiga-tion of the dielectric properties and of the viscosity of the solutions enables the study of the induced conformational changes.
Relipidated BSA is characterized by a higher mobility on agar gel electrophoresis than the native and delipidated samples. The relipidated BSA molecule becomes more spherical, its equivalent volume increases and its dipole moment decreases through fatty acid addition, whereas its intrinsic viscosity remains unchanged.