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Avidin column as a highly efficient and stable alternative for immobilization of ligands for affinity chromatography
Author(s) -
Bayer Edward A.,
Wilchek Meir
Publication year - 1990
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300030303
Subject(s) - affinity chromatography , avidin , biotinylation , chemistry , sepharose , chromatography , biotin , lectin , transferrin , adsorption , biochemistry , organic chemistry , enzyme
Abstract The avidin/biotin system was applied as a general mediator in the adsorption/desorption or immobilization of biologically active macromolecules to solid supports. In this context, model biotinylated proteins (lectins and antibodies) were attached to avidin‐coupled Sepharose. As examples for affinity chromatography, peanut agglutinin and anti‐transferrin antibody were used to isolate asialofetuin and transferrin, respectively. The capacity and product yields were significantly better than those achieved with conventional affinity chromatography on CNBr‐activated Sepharose columns containing the same lectin or antibody. Moreover, the columns were characterized by improved stability properties exhibiting remarkably low levels of leakage.