Gewählte Publikation:
Keuper, HJ; Klein, RA; Spener, F.
The analysis of fatty acid binding to protein using a modified equilibrium dialysis method: detailed analysis of chromophore-fatty acid-protein interactions.
Chem Phys Lipids. 1983; 32(2):153-164
Doi: 10.1016/0009-3084(83)90050-6
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- Co-Autor*innen der Med Uni Graz
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Spener Friedrich
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- Abstract:
- 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.
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Binding Sites -
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Dialysis - methods
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Kinetics -
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Oleic Acid -
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Oleic Acids - metabolism
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Permeability -
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Protein Binding -
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Proteins - metabolism