Chromatography of plasma proteins on immobilized Cibacron Blue F3-GA. Mechanism of the molecular interaction.
Fractionation of plasma proteins on immobilized Cibacron Blue F3-GA (Affi-gel Blue) under different conditions of pH, ionic strength and temperature was studied. At acidic pH the unbound proteins were eluted in order of increasing pI (the Affi-gel Blue behaving as ion-exchanger); at basic pH and at low ionic strength they were eluted in order of decreasing molecular weight (separation by diffusion-exclusion). For the proteins that were either retarded in comparison with substances of similar molecular characteristics, or that were bound to the resin, pseudo-ligand affinity or hydrophobic interactions were also implicated.
D000873:Anthracenes; D001798:Blood Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D011487:Protein Conformation; D013696:Temperature; D014227:Triazines
D000873:Anthracenes; D001798:Blood Proteins; D014227:Triazines; C012842:Cibacron Blue F 3GA