Immobilized Metal-Ion Affinity Chromatography

Тодорова, Даниела; Vijayalakshmi, M.A.

doi:10.1201/9780824751982.ch10

Cited by 5 publications

(20 citation statements)

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“…Many binding agents have been utilized as stationary phases in affinity chromatography. As shown in Figure 6, this method has made use of both naturally-occurring binding agents and non-biological ligands [1][2][3][4][5]100,[114][115][116][117][118][126][127][128][129][130][131]. Natural binding agents employed in affinity chromatography have included enzymes, antibodies, antigens, immunoglobulin-binding proteins, biotin plus avidin or streptavidin, lectins, serum proteins, carbohydrates, lipids, and nucleic acids [1][2][3][4][5]84,100].…”

Section: Binding Agents In Affinity Chromatographymentioning

confidence: 99%

“…Natural binding agents employed in affinity chromatography have included enzymes, antibodies, antigens, immunoglobulin-binding proteins, biotin plus avidin or streptavidin, lectins, serum proteins, carbohydrates, lipids, and nucleic acids [1][2][3][4][5]84,100]. Non-biological ligands have included aptamers, dyes, metal ion chelates, MIPs, and boronates [1,[114][115][116][117][118][126][127][128][129][130][131].…”

Section: Binding Agents In Affinity Chromatographymentioning

confidence: 99%

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Affinity chromatography: A review of trends and developments over the past 50 years

Rodriguez

Poddar

Iftekhar

et al. 2020

Journal of Chromatography B

145

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Section: Binding Agents In Affinity Chromatographymentioning

confidence: 99%

Section: Binding Agents In Affinity Chromatographymentioning

confidence: 99%

Affinity chromatography: A review of trends and developments over the past 50 years

Rodriguez

Poddar

Iftekhar

et al. 2020

Journal of Chromatography B

145

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“…IMAC makes use of the specific interactions that can occur between immobilized metal ions and targets such as amino acids, peptides, proteins, and nucleic acids [84–87]. The metal ions are immobilized within a column through the use of chelating agents like iminodiacetic acid, nitrilotriacetic acid, carboxymethylated-aspartic acid, and L-glutamic acid.…”

Section: Immobilized Metal Ion Affinity Chromatographymentioning

confidence: 99%

Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments

Hage

Anguizola

et al. 2012

Journal of Pharmaceutical and Biomedical Analysis

178

127

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Affinity chromatography is a separation technique that has become increasingly important in work with biological samples and pharmaceutical agents. This method is based on the use of a biologically-related agent as a stationary phase to selectively retain analytes or to study biological interactions. This review discusses the basic principles behind affinity chromatography and examines recent developments that have occurred in the use of this method for biomedical and pharmaceutical analysis. Techniques based on traditional affinity supports are discussed, but an emphasis is placed on methods in which affinity columns are used as part of HPLC systems or in combination with other analytical methods. General formats for affinity chromatography that are considered include step elution schemes, weak affinity chromatography, affinity extraction and affinity depletion. Specific separation techniques that are examined include lectin affinity chromatography, boronate affinity chromatography, immunoaffinity chromatography, and immobilized metal ion affinity chromatography. Approaches for the study of biological interactions by affinity chromatography are also presented, such as the measurement of equilibrium constants, rate constants, or competition and displacement effects. In addition, related developments in the use of immobilized enzyme reactors, molecularly imprinted polymers, dye ligands and aptamers are briefly considered.

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“…This is held in place on the column by using it to form a coordination complex with a chelating agent like iminodiacetic acid (IDA) or nitrilotriacetic acid (NTA). This chelating agent is, in turn, covalently linked to the support [75,87].…”

Section: +mentioning

confidence: 99%

Affinity monolith chromatography

Mallik

Hage²

2006

J of Separation Science

190

282

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The combined use of monolithic supports with selective affinity ligands as stationary phases has recently given rise to a new method known as affinity monolith chromatography (AMC). This review will discuss the basic principles behind AMC and examine the types of supports and ligands that have been employed in this method. Approaches for placing affinity ligands in monoliths will be considered, including methods based on covalent immobilization, biospecific adsorption, entrapment, and the formation of coordination complexes. Several reported applications will then be presented, such as the use of AMC for bioaffinity chromatography, immunoaffinity chromatography, immobilized metal-ion affinity chromatography, dye-ligand affinity chromatography, and biomimetic chromatography. Other applications that will be discussed are chiral separations and studies of biological interactions based on AMC.

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Immobilized Metal-Ion Affinity Chromatography

Cited by 5 publications

References 0 publications

Affinity chromatography: A review of trends and developments over the past 50 years

Affinity chromatography: A review of trends and developments over the past 50 years

Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments

Affinity monolith chromatography

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