Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates.

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Research Abstract Details 

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Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Abstract Text:

John F Langford,Xuankuo Xu,Yan Yao,Sean F Maloney,Abraham M Lenhoff,

Intraparticle transport of proteins usually represents the principal resistance controlling their uptake in preparative separations. In ion-exchange chromatography two limiting models are commonly used to describe such uptake: pore diffusion, in which only free protein in the pore lumen contributes to transport, and homogeneous diffusion, in which the transport flux is determined by the gradient in the total protein concentration, free or adsorbed. Several studies have noted a transition from pore to homogeneous diffusion with increasing ionic strength in some systems, and here we investigate the mechanistic basis for this transition. The studies were performed on a set of custom-synthesized methacrylate-based strong cation exchangers differing in ligand density into which uptake of two proteins was examined using confocal microscopy and frontal loading experiments. We find that the transition in uptake mechanism occurs in all cases studied, and generally coincides with an optimum in the dynamic binding capacity at moderately high flow rates. The transition appears to occur when protein-surface attraction is weakened sufficiently, and this is correlated with the isocratic retention factor k' for the system of interest: the transition occurs in the vicinity of k' approximately 3000. This result, which may indicate that adsorption is sufficiently weak to allow the protein to diffuse along or near the surface, provides a predictive basis for optimizing preparative separations using only isocratic retention data.

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Publishing Authors By Initials

JF Langford,X Xu,Y Yao,SF Maloney,AM Lenhoff,

For similar proteins research abstracts see: proteins research

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Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of chromatography. A

VOLUME: 1163

Page Numbers: 190-202

Journal Abbreviation:

ISSN: 0021-9673

DAY: 22

MONTH: 06

YEAR: 2007

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9318488

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates. Information

Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates.

AFFILIATION: Department of Chemical Engineering, University of Delaware, Newark, DE 19716, USA.

Country: Netherlands

AGENCY: United States NCRR

GRANT: P20 RR16472

ACRONYM: RR

MEDLINETA: J Chromatogr A

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