Clonis Y D
Department of Chemistry, University of Patras, Patras, Greece.
Methods Mol Biol. 1992;11:105-23. doi: 10.1385/0-89603-213-2:105.
Affinity chromatography (1,2), the most powerful of all protein-fractionation techniques, relies on the formation of reversible specific complexes between a ligand immobilized on an insoluble polymer support, termed affinity adsorbent, and the species to be isolated free in solution. The modern support materials (natural, synthetic, or inorganic), consist of macroporous hydrophilic beaded particles, usually bearing free hydroxyl groups available for ligand immobilization. When the support is made of noncompressible particles of small diameter (e.g., 5-20 µm) and narrow size distribution (e.g., 0.2-2 µm) the technique is termed high-performance affinity chromatography (HPAC) (3-5).
亲和色谱法(1,2)是所有蛋白质分离技术中最强大的一种,它依赖于固定在不溶性聚合物载体(称为亲和吸附剂)上的配体与溶液中游离的待分离物质之间形成可逆的特异性复合物。现代载体材料(天然、合成或无机)由大孔亲水性珠状颗粒组成,通常带有可用于固定配体的游离羟基。当载体由小直径(例如5-20 µm)且尺寸分布窄(例如0.2-2 µm)的不可压缩颗粒制成时,该技术称为高效亲和色谱法(HPAC)(3-5)。