Comparison of chromatographic ion-exchange resins

Staby, Arne; Jacobsen, Jan H.; Hansen, Ronni G.; Bruus, Ulla K.; Jensen, Inge Holm

doi:10.1016/j.chroma.2006.03.116

Cited by 76 publications

(28 citation statements)

References 37 publications

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“…A wide variety of materials have been prepared for protein separation and purification in ion-exchange mode, with common and commercially available supports typically containing carboxylate functional groups as weak cation exchangers, and sulfonate functional groups as strong cation exchangers. Comparative studies of commercial ion exchange sorbents show the vast number of materials available [1]. The introduction of ion-exchange functionality can be accomplished by a number of different strategies such as coating procedures [2], and "grafting from" [3,4] and "grafting to" alternatives [5] including the use of ring-opening methathesis polymerization [6].…”

Section: Introductionmentioning

confidence: 99%

A cation‐exchange material for protein separations based on grafting of thiol‐terminated sulfopropyl methacrylate telomers onto hydrophilized monodisperse divinylbenzene particles

Nordborg¹,

Limé²,

Shchukarev³

et al. 2008

J of Separation Science

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A strong cation-exchange separation material has been prepared from monodisperse divinylbenzene particles modified by a "grafting to" approach, utilizing as anchoring points epoxy groups introduced onto the surface of the particles via oxidation of residual vinyl groups. The grafted chains consisted of thiol-terminated telomers of sulfopropyl methacrylate prepared by iniferter mediated polymerization, and grafting was performed by reaction of the corresponding thiolate anion with the surface epoxy groups. Attachment through epoxy moieties that were subsequently converted into 2,3-propanediol groups increased the hydrophilicity of the polymeric particles and incubation experiments showed no signs of the proteins denaturing on the column during an extended contact time of 1 h at room temperature. The performance of the grafted material was demonstrated by the chromatographic separation of cytochrome C, lysozyme, myoglobin, and ribonuclease A, in a cation-exchange mode.

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Section: Introductionmentioning

confidence: 99%

A cation‐exchange material for protein separations based on grafting of thiol‐terminated sulfopropyl methacrylate telomers onto hydrophilized monodisperse divinylbenzene particles

Nordborg¹,

Limé²,

Shchukarev³

et al. 2008

J of Separation Science

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show abstract

“…After the column was saturated, it was flushed with 20 mM phosphate buffer (pH 7. [57,58], but is almost two times higher than that obtained for a tetrazole-functionalized ion exchanger [59]. This comparable dynamic binding capacity is presumably due to the high amount of SPMA used in the copolymerization.…”

Section: Dynamic Binding Capacitymentioning

confidence: 43%

Polymeric strong cation‐exchange monolithic column for capillary liquid chromatography of peptides and proteins

Chen

Tolley

Lee³

2009

J of Separation Science

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A strong cation-exchange (SCX) monolithic stationary phase was prepared in 75 microm id capillaries by direct in situ polymerization of sulfopropyl methacrylate and polyethylene glycol diacrylate in a ternary porogen system consisting of methanol, cyclohexanol, and water. The resulting monolith exhibited good dynamic binding capacity, fast kinetic adsorption of proteins, and high permeability. The monolith had a dynamic binding capacity of approximately 52 mg/mL of column volume for lysozyme and cytochrome C. The monolith was evaluated for SCX capillary LC of synthetic peptides, natural peptides, and protein standards. Fast separation of proteins was achieved in less than 4 min. The average peak capacity for peptides was 28 using a relatively steep gradient when hydrophobic interactions were suppressed with 40% acetonitrile.

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“…Batch experiments are used for measurement of static capacities and uptake curves [5]. Staby et al have investigated 23 chromatographic anionexchange resins [6][7][8] and 25 chromatographic weak and strong cation-exchange resins [9][10][11] comprising 7400 measurements. The particle size ranges from 20 to 400 m. The proteins used in the investigation include lipolase (pI 4.3), BSA (pI 5-5.2), insulin precursor (pI 5.3), anti-FVII Mab (IgG) (pI 6-7), myoglobin (pI 7-8), aprotinin (pI ∼ 10.5), and lysozyme (pI ∼ 11) and cover a broad range of isoelectric points.…”

Section: Conventional Screening Methodsmentioning

confidence: 99%

Development, modelling, optimisation and scale-up of chromatographic purification of a therapeutic protein

Mollerup

Hansen

Kidal

et al. 2007

Fluid Phase Equilibria

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Comparison of chromatographic ion-exchange resins

Cited by 76 publications

References 37 publications

A cation‐exchange material for protein separations based on grafting of thiol‐terminated sulfopropyl methacrylate telomers onto hydrophilized monodisperse divinylbenzene particles

A cation‐exchange material for protein separations based on grafting of thiol‐terminated sulfopropyl methacrylate telomers onto hydrophilized monodisperse divinylbenzene particles

Polymeric strong cation‐exchange monolithic column for capillary liquid chromatography of peptides and proteins

Development, modelling, optimisation and scale-up of chromatographic purification of a therapeutic protein

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