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.
Chromatography of plasma proteins on immobilized Cibacron Blue F3-GA. Mechanism of the molecular interaction / E. Gianazza, P. Arnaud. - In: BIOCHEMICAL JOURNAL. - ISSN 0006-2936. - 203:3(1982 Jun 01), pp. 637-641. [10.1042/bj2030637]
Chromatography of plasma proteins on immobilized Cibacron Blue F3-GA. Mechanism of the molecular interaction
E. GianazzaPrimo
;
1982
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.File | Dimensione | Formato | |
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