TY - JOUR
T1 - Pharmaceutical and biomedical applications of affinity chromatography
T2 - Recent trends and developments
AU - Hage, David S.
AU - Anguizola, Jeanethe A.
AU - Bi, Cong
AU - Li, Rong
AU - Matsuda, Ryan
AU - Papastavros, Efthimia
AU - Pfaunmiller, Erika
AU - Vargas, John
AU - Zheng, Xiwei
N1 - Funding Information:
This research was supported, in part, by the National Institutes of Health under grants R01 DK069629 and R01 GM044931 and by the NSF/EPSCoR program under grant EPS-1004094 .
PY - 2012/10
Y1 - 2012/10
N2 - 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.
AB - 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.
KW - Affinity chromatography
KW - Boronate affinity chromatography
KW - Immobilized metal ion affinity chromatography
KW - Immunoaffinity chromatography
KW - Lectin affinity chromatography
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U2 - 10.1016/j.jpba.2012.01.004
DO - 10.1016/j.jpba.2012.01.004
M3 - Review article
C2 - 22305083
AN - SCOPUS:84865075245
SN - 0731-7085
VL - 69
SP - 93
EP - 105
JO - Journal of Pharmaceutical and Biomedical Analysis
JF - Journal of Pharmaceutical and Biomedical Analysis
ER -