Affinity partitioning of albumin and α-fetoprotein in an aqueous two-phase system using poly(ethylene glycol)-bound triazine dyes
✍ Scribed by G. Birkenmeier; E. Usbeck; G. Kopperschläger
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 628 KB
- Volume
- 136
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
Human albumin and alpha-fetoprotein are partitioned in an aqueous two-phase system composed of 10% (w/w) Dextran and 7.5% (w/w) poly(ethylene glycol). When a small amount of poly(ethylene glycol) is replaced by Cibacron Blue F3G-A-liganded poly(ethylene glycol) the partition coefficient, K, of albumin increases by the factor of about 4000 whereas the K value of alpha-fetoprotein undergoes only a small change. The change of the partition coefficient in a logarithmic scale induced by increasing dye-polymer concentrations turned out as a useful measure for the affinity of albumin and alpha-fetoprotein to the dyes. The effect of pH and salt concentration on the affinity partition of albumin and alpha-fetoprotein is demonstrated. The partition of the two proteins in presence of Cibacron Blue F3G-A-liganded poly(ethylene glycol) is compared with seven other triazine dye-poly(ethylene glycol) derivatives.
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