Specific salt effects in hydrophobic interaction chromatography of proteins
✍ Scribed by L. Szepesy; Cs. Horváth
- Book ID
- 112721346
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 418 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0009-5893
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📜 SIMILAR VOLUMES
Pure hydrophobic chromatography can be observed with agarose gels containing .caprylyl/~ydrazide. These nonionic gels show increased avidity in protein adsorption with ~higher content of caprylyl groups. Lyotropic salt effects can :be used to control .chromatographic behavior of proteins. Salting-ou
## Abstract Hydrophobic interaction chromatography (HIC) uses weakly hydrophobic resins and requires a salting‐out salt to promote protein–resin interaction. The salting‐out effects increase with protein and salt concentration. Dynamic binding capacity (DBC) is dependent on the binding constant, as