Affinity partitioning of albumin and alpha-fetoprotein in an aqueous two-phase system using poly(ethylene glycol)-bound triazine dyes

Anal Biochem. 1984 Jan;136(1):264-71. doi: 10.1016/0003-2697(84)90334-8.

Abstract

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.

MeSH terms

  • Charcoal
  • Chromatography, Affinity / methods
  • Coloring Agents
  • Humans
  • Hydrogen-Ion Concentration
  • Iodine Radioisotopes
  • Isotope Labeling
  • Polyethylene Glycols
  • Serum Albumin / analysis*
  • Triazines
  • alpha-Fetoproteins / analysis*

Substances

  • Coloring Agents
  • Iodine Radioisotopes
  • Serum Albumin
  • Triazines
  • alpha-Fetoproteins
  • Charcoal
  • Polyethylene Glycols