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 40
A modified equilibrium dialysis method for studying fatty acid binding to proteins
β Scribed by R.A. Klein; H.J.K. Keuper
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 492 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0009-3084
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β¦ Synopsis
A modified equilibrium dialysis method is described which is suitable for investigating the binding of fatty acids in the form of aqueous micellar dispersions to proteins. The method uses a permeant chromophore which complexes reversibly with free fatty acid within the dialysis bag. The concentration outside the dialysis bag is determined spectrophotometrically. Binding of oleic acid to bovine serum albumin is given as an example. A simplified analysis of fatty acid binding is given and used to indicate the potential of the method.
π SIMILAR VOLUMES
Vesicles having diameters from 20 to 200 nm were prepared from egg-yolk phosphatidylcholine (PC) and were separated as well as analyzed by methods that can be carried out with standard laboratory equipment. Gel-chromatography on Sephacryl S 1000 was adapted for expeditious size analysis of vesicles