Modeling of immunoglobulin uptake by N,N,N′,N′- ethylenediaminetetramethylenephosphonic acid-modified zirconia particles under static and dynamic conditions

Sabyasachi Sarkar, Anuradha Subramanian

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)81-87
Number of pages7
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume821
Issue number1
DOIs
StatePublished - Jul 5 2005

Fingerprint

Immunoglobulins
Rate constants
Acids
Packed beds
Immunoglobulin A
Kinetics
Immunoglobulin M
Proteins
Immunoglobulin G
Pore size
zirconium oxide
Experiments

Keywords

  • Immunoglobulins
  • Modeling
  • Pseudo-affinity separations
  • Zirconia

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

Cite this

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abstract = "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.",
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