Control of Protein Adsorption in Capillary Electrophoresis via an Irreversibly Bound Protein Coating
✍ Scribed by Paul R. Van Tassel; Dorothée Miras; Agnès Hagege; Maurice Leroy; Jean-Claude Voegel; Pierre Schaaf
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 123 KB
- Volume
- 183
- Category
- Article
- ISSN
- 0021-9797
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✦ Synopsis
Due to the tremendous success exhibited by CE in the
We present a new method of controlling protein adsorption separation of organic and inorganic ions, amino acids, and during capillary electrophoresis which involves placement of a peptides, considerable effort is being put forth to apply this thermally treated monolayer of adsorbed fibrinogen on the internal technique to biological solutions containing larger, more surface of the fused silica capillary. The thermal treatment is complex molecules such as proteins (2-9). Additional effort shown to render the adsorbed layer stable to an applied electric is directed toward exploiting the highly specific binding abilfield. In contrast, an adsorbed layer not receiving thermal treatity of certain proteins by using them as mobile selectors in ment will exhibit steady desorption when exposed to an electric CE separations of chiral mixtures (10-17). The latter offers field. Protein coated capillaries exhibit a surface potential and an electro-osmotic mobility that are (i) 30% smaller that those of great promise to the pharmaceutical industry as biological bare capillaries and (ii) stable over several measurements. Protein enantiomers frequently differ in potency, metabolism, and coated capillaries will likely be useful in bioseparations utilizing pharmacological action.
proteins.
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