TY - JOUR
T1 - Modeling of immunoglobulin uptake by N,N,N′,N′- ethylenediaminetetramethylenephosphonic acid-modified zirconia particles under static and dynamic conditions
AU - Sarkar, Sabyasachi
AU - Subramanian, Anuradha
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/7/5
Y1 - 2005/7/5
N2 - A matrix developed from N,N,N′,N′- ethylenediaminetetramethylenephosphonic acid-modified zirconia beads (further referred to as r_PEZ); 25-38 μm in diameter and with a pore size of 22 ± 3 nm, was utilized for the separation of immunoglobulins (Igs). r_PEZ has been shown to bind to various Igs originating from a wide variety of species. To understand the mechanisms controlling the uptake of Igs by r_PEZ, static protein uptake experiments were carried out. The protein uptake profiles were further modeled with a kinetic rate constant model. Individual studies were undertaken for human immunoglobulin A, G and M (HIgA, HIgG and HIgM). The kinetic rate constant model indicated that HIgG binding to r_PEZ was more favorable than its disassociation. The equilibrium rate constants were found to decrease with increasing concentration. The effect of continuous loading in a packed bed system utilizing r_PEZ matrix was evaluated by carrying out frontal studies, using different feed concentrations and linear velocities. The breakthrough profiles obtained for the uptake of HIgG were modeled with the pore diffusion model. The model was found to best describe the breakthrough profiles obtained at a feed concentration of 2.0 mg of HIgG per milliliter. The NTU for the packed bed was found to be equal to 2.
AB - A matrix developed from N,N,N′,N′- ethylenediaminetetramethylenephosphonic acid-modified zirconia beads (further referred to as r_PEZ); 25-38 μm in diameter and with a pore size of 22 ± 3 nm, was utilized for the separation of immunoglobulins (Igs). r_PEZ has been shown to bind to various Igs originating from a wide variety of species. To understand the mechanisms controlling the uptake of Igs by r_PEZ, static protein uptake experiments were carried out. The protein uptake profiles were further modeled with a kinetic rate constant model. Individual studies were undertaken for human immunoglobulin A, G and M (HIgA, HIgG and HIgM). The kinetic rate constant model indicated that HIgG binding to r_PEZ was more favorable than its disassociation. The equilibrium rate constants were found to decrease with increasing concentration. The effect of continuous loading in a packed bed system utilizing r_PEZ matrix was evaluated by carrying out frontal studies, using different feed concentrations and linear velocities. The breakthrough profiles obtained for the uptake of HIgG were modeled with the pore diffusion model. The model was found to best describe the breakthrough profiles obtained at a feed concentration of 2.0 mg of HIgG per milliliter. The NTU for the packed bed was found to be equal to 2.
KW - Immunoglobulins
KW - Modeling
KW - Pseudo-affinity separations
KW - Zirconia
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U2 - 10.1016/j.jchromb.2005.04.002
DO - 10.1016/j.jchromb.2005.04.002
M3 - Article
C2 - 15919247
AN - SCOPUS:20344377863
SN - 1570-0232
VL - 821
SP - 81
EP - 87
JO - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
JF - Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
IS - 1
ER -