The adsorption of human serum albumin (HSA) on various types of chromatogra
phic support (C6 reversed-phase, anion-exchanger, immunoadsorbent) was stud
ied by analysis of frontal breakthrough curves. These curves are first char
acterized by a sharp increase; a more diffuse profile is then observed at l
onger elution times. Data were analyzed using a bi-Langmuir kinetic model a
ssuming irreversible adsorption on two types of binding site. Fitting the m
odel to the experimental data enables determination of apparent adsorption
rates and the saturation capacities of both types of binding site.