Predicting the elution behavior of proteins in affinity chromatography on non-porous particles

Lee, Wen‐Chien; Chen, Chi-Hao

doi:10.1016/s0165-022x(01)00189-0

Cited by 10 publications

(9 citation statements)

References 29 publications

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“…A good fit between the experimental data and best-fit peaks was obtained, giving an estimated dissociation rate constant of 1.5 s -1 for IgG from protein A in the presence of a pH 3.0 buffer [30]. The same technique has also utilized in examining the elution of lysozyme from a Cibacron Blue 3GA columns in the presence of elution buffers that contain various concentrations of sodium chloride [29]. …”

Section: Peak Fitting Methodsmentioning

confidence: 99%

“…Similarly, work in Refs. [29, 30] that has examined analyte dissociation kinetics from affinity columns has assumed that the contribution of stagnant mobile phase mass transfer to the apparent rate of analyte desorption is negligible. It is for this reason that the rate constants determined by this technique are typically apparent values that are actually a function or more than one kinetic process occurring within the column.…”

Section: Peak Fitting Methodsmentioning

confidence: 99%

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Kinetic studies of biological interactions by affinity chromatography

Schiel

Hage²

2009

J of Separation Science

183

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The rates at which biological interactions occur can provide important information on the mechanism and behavior of such processes in living systems. This review will discuss how affinity chromatography can be used as a tool to examine the kinetics of biological interactions. This approach, referred to here as biointeraction chromatography, uses a column with an immobilized binding agent to examine the association or dissociation of this agent with other compounds. The use of HPLC-based affinity columns in kinetic studies has received particular attention in recent years. Advantages of using HPLC with affinity chromatography for this purpose include the ability to reuse the same ligand within a column for a large number of experiments, and the good precision and accuracy of this approach. A number of techniques are available for kinetic studies through the use of affinity columns and biointeraction chromatography. These approaches include plate height measurements, peak profiling, peak fitting, split-peak measurements, and peak decay analysis. The general principles for each of these methods are discussed in this review and some recent applications of these techniques are presented. The advantages and potential limitations of each approach are also considered.

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Section: Peak Fitting Methodsmentioning

confidence: 99%

Section: Peak Fitting Methodsmentioning

confidence: 99%

Kinetic studies of biological interactions by affinity chromatography

Schiel

Hage²

2009

J of Separation Science

183

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“…This method has also been applied to investigate the rate constants and types of binding sites for drug interactions with β 2 -AR (Li et al, 2015; Liang et al, 2018) and to examine drug binding with β-cyclodextrin with detection based on mass spectrometry (Wang et al, 2016). Similar peak fitting approaches have been described for kinetic studies of IgG with immobilized protein A during elution at pH 3.0 and to determine rate constants for the binding of lysozyme with immobilized Cibacron Blue 3GA at various concentrations of sodium chloride (Lee and Chuang, 1996; Lee and Chen, 2001).…”

Section: Peak Fittingmentioning

confidence: 99%

Kinetic Analysis by Affinity Chromatography

2019

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Important information on chemical processes in living systems can be obtained by the rates at which these biological interactions occur. This review will discuss several techniques based on traditional and high-performance affinity chromatography that may be used to examine the kinetics of biological reactions. These methods include band-broadening measurements, techniques for peak fitting, split-peak analysis, peak decay studies, and ultrafast affinity extraction. The general principles and theory of each method, as applied to the determination of rate constants, will be discussed. The applications of each approach, along with its advantages and limitations, will also be considered.

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“…Related peak fitting methods have been utilized to estimate the dissociation rate constant for IgG from immobilized protein A in the presence of a pH 3.0 buffer [127]. A similar approach has been utilized to examine the elution of lysozyme from a Cibacron Blue 3GA column in the presence of buffers that contained various concentrations of sodium chloride [128]. …”

Section: Affinity Chromatographymentioning

confidence: 99%

“…The association and dissociation rate constants that have been measured by peak fitting have been in the range of 10 4 to 10 7 M −1 s −1 and 10 −1 to 10 s −1 , respectively [106,116,123,128,131,132]. However, it is necessary to test and verify any assumptions that are made in this approach, such as whether mobile phase mass transfer is negligible or needs to be considered when examining the rate of a target’s interaction with the immobilized binding agent [106,129–131].…”

Section: Affinity Chromatographymentioning

confidence: 99%

Analytical methods for kinetic studies of biological interactions: A review

Zheng

Zhao

et al. 2015

Journal of Pharmaceutical and Biomedical Analysis

142

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The rates at which biological interactions occur can provide important information concerning the mechanism and behavior of these processes in living systems. This review discusses several analytical methods that can be used to examine the kinetics of biological interactions. These techniques include common or traditional methods such as stopped-flow analysis and surface plasmon resonance spectroscopy, as well as alternative methods based on affinity chromatography and capillary electrophoresis. The general principles and theory behind these approaches are examined, and it is shown how each technique can be utilized to provide information on the kinetics of biological interactions. Examples of applications are also given for each method. In addition, a discussion is provided on the relative advantages or potential limitations of each technique regarding its use in kinetic studies.

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Predicting the elution behavior of proteins in affinity chromatography on non-porous particles

Cited by 10 publications

References 29 publications

Kinetic studies of biological interactions by affinity chromatography

Kinetic studies of biological interactions by affinity chromatography

Kinetic Analysis by Affinity Chromatography

Analytical methods for kinetic studies of biological interactions: A review

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