The effect of in-place regeneration on equilibrium and kinetic charact
eristics of the adsorption of bovine serum albumin to a DEAE-cellulose
anion exchanger has been determined. Regeneration with sodium hydroxi
de and time of exposure showed no effect on equilibrium behavior. Brea
kthrough curves were measured for protein adsorption on fixed-bed colu
mns and analyzed by a simple model to determine the relevant rate cons
tants for the adsorption process. It was found that forward adsorption
rate constant decreased exponentially with the chemical treatment exp
osure time. The implications of the results on the design and optimiza
tion of ion-exchange chromatographic processes are discussed. (C) 1997
Elsevier Science B.V.