Chromatography of plasma proteins on immobilized Cibacron Blue F3-GA. Mechanism of the molecular interaction

Biochem J. 1982 Jun 1;203(3):637-41. doi: 10.1042/bj2030637.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anthracenes*
  • Blood Proteins / isolation & purification*
  • Chromatography, Affinity / methods*
  • Hydrogen-Ion Concentration
  • Osmolar Concentration
  • Protein Conformation
  • Temperature
  • Triazines*

Substances

  • Anthracenes
  • Blood Proteins
  • Triazines
  • Cibacron Blue F 3GA