Biopolymer affinity chromatography

Affinity chromatography, first described by Cuatrecasas et al.,U9 utilizes the ability of a protein or another biopolymer to recognize a natural or synthetic ligand. The affinity chromatography sorbent consists of a porous matrix itself on which a ligand is chemically immobilized directly or by means of a spacer arm. 

Zhou D, Zou H, Ni J, Wang H, Yang L, and Zhang Y. Membrane affinity chromatography for analysis and purification of biopolymers. Chromatographia 1999 50 23-27. 

Classical LLPC using aqueous-aqueous polymer systems based on Albertsson s [9] PEG-dextran system has provided a versatile tool for the separation of proteins and nucleic acids, thus increasing the arsenal of biopolymer purification methods currently dominated by gel filtration, ion-exchange chromatography, and affinity chromatography RPC. The technique operates... 

Wainer, 1. W. Enantioselective high-performance liquid affinity chromatography as a probe ofligand-biopolymer interactions an overview of a different use for high-performance liquid chromatographic chiral stationary phases,... 

These biopolymers can be used for the immobilization of metal ions not only with the final objective of metal recovery (and subsequent valorization by desorption or chemical/thermal destmction of the polymer matrix) but also for elaborating new materials or designing new applications. Depending on the metal immobilized on the biopolymer, it is possible to design new sorbents (immobilization of iron on alginate [119], of molybdate on chitosan [59], for As(V) removal, of silver on chitosan for pesticide removal [120]), supports for affinity chromatography [121], antimicrobial material [122], drug release material [123], neutron capture therapy [124], and photoluminescent materials [125]. These are only a few... 

Available functional groups are listed in Table 7.1. Silica can also be functionalized with groups suitable for ion exchange, affinity chromatography or the separation of enantiomers. The choice of special phases for the separation of biopolymers is immense. 

Metal interaction chromatography is an HPLC technique that can separate many biopolymers because of their differential ability to form complexes with metal ions [1]. It employs a stationary phase with an appropriate metal immobilized via chelating functions bound to the surface. Retention and separation of the sample components occur largely by their interaction with the chelated metal. Although immobilized metal affinity chromatography (IMAC) is a common name for the technique, it is called metal interaction chromatography (MIC) in this book to conform to the nomenclature used for the other interactive chromatographic methods for biopolymer separation by HPLC. 

Gold, E. W. (1980). An interaction of albumin with hyaluronic acid and chondroitin sulfate A study of affinity chromatography and circular di-chioism. Biopolymers 9, 1407-1414. 

Topics of interest in relation to biopolymer surface modifications have already been addressed before. As these topics have continuously been reviewed during the last 30 years of polymer chemistry, the synthetic methods that were used most are covered here. This chapter emphasizes in particular the physical/chemical modifications necessary to improve the apphcation properties of biopolymers and hence their potential applications in drug dehvery systems, packaging, affinity chromatography, and biosensor fields. 

Although most of the biopolymers used as affinity chromatography supports are polysaccharides, other biomolecules also have been reported. Purification of... 

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