The analysis of fatty acid binding to protein using a modified equilibrium dialysis method: detailed analysis of chromophore—fatty acid—protein interactions

✍ Scribed by H.J.K. Keuper; R.A. Klein; F. Spener

• Publisher: Elsevier Science
• Year: 1983
• Tongue: English
• Weight: 496 KB
• Volume: 32
• Category: Article
• ISSN: 0009-3084
• DOI: 10.1016/0009-3084(83)90050-6

✦ Synopsis

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 gl and 400 ~tl 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 micromethods of dialysis are compared, and the binding of fatty acid to bovine serum albumin and ~4actoglobulin 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.