Gibbs free energy of adsorption for biomolecules in ion-exchange systems
References (31)
- et al.
- et al.
J. Chromatogr.
(1983) - et al.
J. Chromatogr.
(1992) - et al.
J. Chromatogr.
(1993) - et al.
J. Chromatogr.
(1993) - et al.
J. Chromatogr.
(1984) - et al.
J. Chromatogr.
(1986) - et al.
J. Chromatogr.
(1989) - et al.
J. Chromatogr.
(1986) - et al.
J. Chromatogr.
(1988)
J. Chromatogr.
(1993)
Reactive Polym.
(1989)
Advan. Protein Chem.
(1979)
Anal. Chem.
(1991)
Anal. Chem.
(1992)
Cited by (42)
Opportunity for a greener recovery of dysprosium(III) from secondary sources by a novel Mannich reaction-modified phosphorylated chitosan hydrogel
2024, International Journal of Biological MacromoleculesA novel approach to calculate protein adsorption isotherms by molecular dynamics simulations
2020, Journal of Chromatography AAdsorptive behavior of α-lactalbumin on cation-exchange supermacroporous monolithic column
2015, Fluid Phase EquilibriaCitation Excerpt :Many parameters, as pH, temperature, type and amount of salts, affects protein adsorption and only the knowledge of these effects allows a rational improvement of it [36]. Calorimetric techniques, mathematical correlations, computational modeling and others have been made in order to elucidate these mechanisms and their implications on the structure of proteins [8,36,39–42]. The protein ion-exchange process is not only controlled by interactions among opposite charges.
- 1
Current address: PerSeptive Biosystems, 12 Emily Street, Cambridge, MA 02139, USA.
Copyright © 1994 Published by Elsevier B.V.