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Adsorption equilibrium in immuno-affinity chromatography with polyclonal and monoclonal antibodies

✍ Scribed by Eizo Sada; Shigeo Katoh; Kiyoshi Sukai; Masaaki Tohma; Akihiko Kondo

Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
493 KB
Volume
28
Category
Article
ISSN
0006-3592

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✦ Synopsis

The effects of pH, ionic strength, anion species, and antibody concentration on t h e adsorption equilibrium between immobilized antibodies and antigens were studied by use of anti-BSA, anti-HSA, anti-BlgG, and monoclonal anti-HSA coupled to Sepharose 4B. The polyclonal antibodies possessed average binding affinities of the order of 108M-', and the heterogeneity was accounted for by assuming a normal distribution of the free energy of antibody-antigen combination. The monoclonal antibody, on the other hand, showed a homogeneous affinity of the Langmuir type. Bound antigens could be eluted by lowering pH or adding a chaotropic anion, and their purity was very high. The antibody ligand was sufficiently stable for repeated use.

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