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. Gianazza
Primo
;
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.
Osmolar Concentration ; Chromatography, Affinity ; Blood Proteins ; Hydrogen-Ion Concentration ; Anthracenes ; Temperature ; Triazines ; Protein Conformation
Settore BIO/10 - Biochimica
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1158278/?tool=pubmed
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/180204
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