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. 1982 Jun 1;203(3):637–641. doi: 10.1042/bj2030637

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

E Gianazza, P Arnaud
PMCID: PMC1158278  PMID: 7115305

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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