Practical Protein Chemistry - A. Darbre 1989

Affinity Chromatography of Proteins
Introduction

A. D. STROSBERG (Molecular Immunology Laboratory, IRBM — CNRS and University of Paris VII, Place Jussieu 2, Paris 75251, France)

Affinity Chromatography, one of the primary Methods for Protein Purification, relies on the specific interaction between two biologically active molecules, one of which is typically covalently linked to an inert matrix. Affinity chromatography is widely used to purify Proteins—such as Antibodies, Enzymes, Hormones, and receptors—as well as other Biopolymers like Polysaccharides and Nucleic Acids, along with larger biological structures including Viruses and Cells.

This chapter addresses practical issues and challenges that arise at various Stages of the experiment. A schematic Overview of the different steps involved in affinity chromatography is presented in Fig. 5.1.

Readers seeking a more detailed Structure/133.html">Discussion of the THEORETICAL FOUNDATIONS OF affinity chromatography may refer to the literature listed at the end of the chapter.



Last update: 06/08/2026

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