Thermodynamic model for electrostatic-interaction chromatography of proteins.
A thermodynamic model derived by Record et al. [M. T. Record, Jr., Biopolymers, 14 (1975) 2137 and M. T. Record, Jr., C. F. Anderson and T. M. Lohman, Q. Rev. Biophys., 11 (1978) 103] from Wyman's linkage theory [J. Wyman, Adv. Protein Chem., 19 (1964) 223] using Manning's condensation model [J. Manning, J. Chem. Phys., 51 (1969) 924] was extended to electrostatic interaction chromatography. Mixed, electrostatic and hydrophobic interactions of a model protein, ovalbumin were characterized by ion and water release.
Mazsaroff
I
I
PerSeptive Biosystems, Inc., Cambridge, MA 02139.
Vàrady
L
L
Mouchawar
G A
GA
Regnier
F E
FE
D002845:Chromatography / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D010047:Ovalbumin / Q000032:analysis; D011094:Polyethyleneimine / Q000032:analysis; D011506:Proteins / Q000032:analysis*; D013816:Thermodynamics
D011506:Proteins; D011094:Polyethyleneimine; D010047:Ovalbumin