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By Sameh Magdeldin

ISBN-10: 9535103253

ISBN-13: 9789535103257

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J Chromatogr B Analyt Technol Biomed Life Sci 805: 361-363 Campbell DH, Luescher E, Lerman LS (1951) Immunologic Adsorbents: I. Isolation of Antibody by Means of a Cellulose-Protein Antigen. Proc Natl Acad Sci U S A 37: 575-578 Casey JL, Coley AM, Foley M (2008) Phage display of peptides in ligand selection for use in affinity chromatography. Methods Mol Biol 421: 111-124 Chen J, Hage DS (2004) Quantitative analysis of allosteric drug-protein binding by biointeraction chromatography. Nat Biotechnol 22: 1445-1448 Clonis YD (2006) Affinity chromatography matures as bioinformatic and combinatorial tools develop.

G. , 2011; Sheldon, 2007). As one example for all we can mention β-D-galactosidase representing an enzyme very popular in food industry applications. Its importance for the milk processing lies in its ability to hydrolyse lactose, as this ability offers the possibility of lactose free milk preparation, an important product for lactose-intolerant people. The ability of some of these enzymes to catalyze transglycosylation reactions is often utilized for health beneficial galactooligosaccharides production.

32 a. Affinity Chromatography Covalent binding For covalent binding of the protein to the carrier amino acid residues not involved in the reaction mechanism may be used. Generally used functional groups are amino groups of lysines and arginines, sulphydryl groups of cysteins, carboxyl groups of aspartic and glutamic acids and hydroxyl groups of tyrosines, serines and threonines. , 1998; Sheldon, 2007). b. g. hydrogen bonds, hydrophobic interactions and van der Waals forces) are involved in the immobilization process.

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Affinity chromatography by Sameh Magdeldin


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