## Abstract The behavior of a series of pure proteins partitioned in aqueous two‐phase systems is compared with their behavior during mild hydrophobic interaction chromatography (HIC). A simple theoretical rationale for this comparison is presented based upon solvophobic theory. Similarities were f
✦ LIBER ✦
An aqueous two-phase system of dextran/hydroxypropyldextran as a model in adsorption studies of Sephadex® gels
✍ Scribed by K. Lampert; H. Determann
- Publisher
- Elsevier Science
- Year
- 1971
- Tongue
- English
- Weight
- 204 KB
- Volume
- 63
- Category
- Article
- ISSN
- 1873-3778
No coin nor oath required. For personal study only.
✦ Synopsis
To investigate this we used monoethyl diglycol ether as the ~eluant and :Se@hodlex LH-20 as the gel since it gives the strongest adsorption effects ,of *all the Se@a:adex gel@. Fig. 2 shows that phenol is eluted before water, both without retardartiion,, ~%~iiclln means well before the total volume of the column (t/'t). Table I gives (data :about :sonne more substances run with this eluant on Sephades LH-20. The basic ckitietion off tillale separation in this solvent should be that of size difference only., .as in common :geIl chromatography.
📜 SIMILAR VOLUMES
On the use of mild hydrophobic interacti
✍
J. G. Huddleston; R. Wang; A. Lyddiatt
📂
Article
📅
1994
🏛
John Wiley and Sons
🌐
English
⚖ 914 KB