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Keywords
(11)
Bovine Serum Albumin
Comparative Study
Flow Rate
High Pressure
Ion Exchange Resin
Monoclonal Antibody
Particle Size Distribution
Process Development
High Salt
Immunoglobulin G
Ionic Strength
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Comparison of chromatographic ion-exchange resins
Comparison of chromatographic ion-exchange resins,10.1016/S0021-9673(00)00999-7,Journal of Chromatography A,Arne Staby,Inge Holm Jensen
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Comparison of chromatographic ion-exchange resins
(
Citations: 5
)
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Arne Staby
,
Inge Holm Jensen
A
comparative study
was performed on strong anion exchangers to investigate the pH dependence, titration curves, efficiency, binding strength,
particle size
distribution, and static and dynamic capacity of the chromatographic resins. The resins tested included Q Sepharose XL, UNO Q-1, Poros 50 HQ, Toyopearl QAE 550c, Separon HemaBio 1000Q, Q-Cellthru Bigbeads Plus, Q Sepharose HP and Toyopearl SuperQ 650s. Testing was performed with five different proteins: anti-Factor VII
monoclonal antibody
(immunoglobulin G), aprotinin, bovine serum albumin, lipolase and myoglobin. The dependence of pH on retention varies from generally low to very high for proteins with a low isoelectric point (pI). An unexpected binding at pH 7–8 of aprotinin with pI >11 was observed on Separon HemaBio 1000Q. No link between pH dependence on retention and titration curves of the different resins was observed. Efficiency results show the expected trend of higher dependence of the plate height with increasing flow-rate of soft resins compared to resins for medium- and high-pressure operation. No or a very small difference in
particle size distribution
was obtained between new and used resins. Binding to anion-exchange resins as a function of
ionic strength
varies to some extent depending on the specific protein. Generally, binding and elution at
high salt
concentration may be performed with Q Sepharose XL, Toyopearl QAE 550c, Q Sepharose HP and Poros 50 HQ, while binding and elution at low salt concentration may be performed with Q-Cellthru Bigbeads Plus. A very high binding capacity was obtained with Q Sepharose XL. Comparison of static capacity and dynamic capacity at 10% breakthrough shows approx. 50–80% utilization of the total available capacity during chromatographic operation. A general good agreement was obtained between this study and data obtained by the suppliers. The results of this study may be used for selection of resins for testing in process development.
Journal:
Journal of Chromatography A - J CHROMATOGR A
, vol. 908, no. 1, pp. 149-161, 2001
DOI:
10.1016/S0021-9673(00)00999-7
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Citations
(5)
High-throughput screening of chromatographic separations: IV. Ion-exchange
(
Citations: 12
)
Brian D. Kelley
,
Mary Switzer
,
Patrick Bastek
,
Jack F. Kramarczyk
,
Kathleen Molnar
,
Tianning Yu
,
Jon Coffman
Journal:
Biotechnology and Bioengineering - BIOTECHNOL BIOENG
, vol. 100, no. 5, pp. 950-963, 2008
Ion exchange chromatography of antibody fragments
(
Citations: 12
)
Anders Ljunglöf
,
Karol M. Lacki
,
Jay Mueller
,
Chithkala Harinarayan
,
Robert van Reis
,
Robert Fahrner
,
James M. Van Alstine
Journal:
Biotechnology and Bioengineering - BIOTECHNOL BIOENG
, vol. 96, no. 3, pp. 515-524, 2007
Effects of salts on protein–surface interactions: applications for column chromatography
(
Citations: 6
)
Kouhei Tsumoto
,
Daisuke Ejima
,
Anna M. Senczuk
,
Yoshiko Kita
,
Tsutomu Arakawa
Journal:
Journal of Pharmaceutical Sciences - J PHARM SCI
, vol. 96, no. 7, pp. 1677-1690, 2007
Protein adsorption on Ion exchange resin: Estimation of equilibrium isotherm parameters from batch kinetic data
(
Citations: 1
)
K. H. Chu
,
M. A. Hashim
Journal:
Biotechnology and Bioprocess Engineering - BIOTECHNOL BIOPROCESS ENG
, vol. 11, no. 1, pp. 61-66, 2006
Properties and Characterization of High Capacity Resins for Biochromatography
(
Citations: 3
)
E. Müller
Journal:
Chemical Engineering & Technology - CHEM ENG TECHNOL
, vol. 28, no. 11, pp. 1295-1305, 2005