2012
DOI: 10.1016/j.jpba.2012.01.004
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Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments

Abstract: 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 … Show more

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Cited by 178 publications
(133 citation statements)
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References 181 publications
(250 reference statements)
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“…Compared with papain and ficin, bromelain is commercially available in the market under name brands such as McCormick and Knorr. Commercial papain, bromelain, and zingibain efficiently hydrolyze a few meat myofibril proteins, such as actomysin, titin, and nebulin, as revealed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) (Hage et al 2012). Sullivan and Calkins (2010) reported that bromelain can improve the sensory evaluation rating and tenderness of meat comparable to other exogenous enzymes.…”
Section: Tenderizationmentioning
confidence: 99%
“…Compared with papain and ficin, bromelain is commercially available in the market under name brands such as McCormick and Knorr. Commercial papain, bromelain, and zingibain efficiently hydrolyze a few meat myofibril proteins, such as actomysin, titin, and nebulin, as revealed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) (Hage et al 2012). Sullivan and Calkins (2010) reported that bromelain can improve the sensory evaluation rating and tenderness of meat comparable to other exogenous enzymes.…”
Section: Tenderizationmentioning
confidence: 99%
“…The purpose of this method is to selectively purify analytics and inspect the biological interactions between molecules. [82][83][84][85] Affinity chromatography was first introduced for the purpose of purification by Cuatecasas, et al in 1968. 86 There are different types of affinity ligands such as protein, enzyme, enzyme substrate or inhibitor, antibody, antigen, hormone, biomimetic dye and etc.…”
Section: Affinity Chromatographymentioning
confidence: 99%
“…Depending on the purpose, selected type of ligand is immobilized within the column and further purification process is done following selective binding. 82 Here we describe some:…”
Section: Affinity Chromatographymentioning
confidence: 99%
“…Notwithstanding, there are three preferred methods for the separation of complex protein or peptide samples in proteomics, including denaturing polyacrylamide gel electrophoresis (PAGE), or sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), twodimensional gel electrophoresis and high-performance liquid chromatography (HPLC). Moreover, other useful tools include capillary electrophoresis and affinity chromatography (Desiderio et al 2010;Hage et al 2012). SDS-PAGE is a preferred technique for protein separation mainly due to its simplicity, reproducibility, as well as acceptable instrumentation and consumable costs.…”
Section: Introductionmentioning
confidence: 99%