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Kenney and Fowell's exceptionally useful new book, Practical Protein Chromatography, brings all the forefront methods of protein separation and purification directly to your laboratory benchtop. The book treats not only powerful analytical separations, but also the small- and large-scale preparative techniques that are currently applicable throughout biological and biomedical research. Chapters, written by experts in each of the techniques covered, treat a variety of methods usable in virtually every laboratory with a chromatographic system. Topics include: immunoaffinity chromatography and selection of antibodies • lectin affinity and dye-ligand chromatography • exploiting weak affinities • alternative coupling chemistries • biospecific affinity elution • size-exclusion HPLC of proteins • chromatofocusing • determination of purity and yield • specialized chromatographic techniques. The established tradition of Methods in Molecular Biology is to present techniques that guarantee optimum results. Everyone doing protein chromatography today-at any level of proficiency-will find Practical Protein Chromatography an indispensable, hands-on guide to the effective use of these methodologies.
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Thiophilic Adsorption Chromatography II William
Hutchens
1. Introduction Thiophilic adsorption is useful for the purification of immunoglobulins under mild conditions (e.g., see ref. I). Although there are several established procedures for the purification of immunoglobulins (Z-5), thiophilic adsorption appears thus far to be unique in its capacity to adsorb three major classes of immunoglobulins (and their subclasses) (68). Furthermore, in contrast to other affinity purification methods (e.g., see refs. 3,4), recovery of the adsorbed (purified) immunoglobulins from the thiophilic adsorption matrix is accomplished efficiently at neutral pH, without the need fo