The analysis of fatty acid binding to protein using a modified equilibrium dialysis method: detailed analysis of chromophore-fatty acid-protein interactions.
In this paper we extend our previous analysis of fatty acid-chromophore-protein interactions using a modified equilibrium dialysis method described previously. A more rigorous mathematical treatment is combined with a micro-dialysis method using a maximum volume of dialyzate of between 250 microliters and 400 microliters to examine the suitability of different chromophores (mepacrine, quinine, chloroquine, chlorpromazine, methylene blue, rhodamine 6G, 6-carboxyfluorescein) for studying the binding of fatty acid to protein. The macro- and micro-methods of dialysis are compared, and the binding of fatty acid to bovine serum albumin and beta-lactoglobulin discussed as examples of the method. Problems associated with propagated errors in the measurements and obtaining the number of binding sites and the binding constants from curve-fitting are also considered.
D001665:Binding Sites; D003956:Dialysis / Q000379:methods; D007700:Kinetics; D019301:Oleic Acid; D009829:Oleic Acids / Q000378:metabolism*; D010539:Permeability; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*
D009829:Oleic Acids; D011506:Proteins; D019301:Oleic Acid