Enzymic oxidation of monoclonal antibodies by soluble and immobilized bifunctional enzyme complexes

Journal of Chromatography
B SolomonG Fleminger

Abstract

Site-specific modification of monoclonal antibodies was achieved by oxidation of the carbohydrate moieties of antibodies which are located remote from the antigen binding sites. Sialic acid and galactose are terminal sugars of these carbohydrate chains. Concomitant treatment of the antibodies with neuraminidase and galactose oxidase generated aldehyde groups in the oligosaccharide moieties of immunoglobulins which reacted selectively with amino or hydrazide groups of the matrix. Subsequent immobilization of neuraminidase and galactose oxidase on Eupergit C-adipic dihydrazide proved to be an efficient and selective system for the enzymic oxidation of the monoclonal antibodies without impairing their immunological activity. Oriented immobilization of enzymically oxidized monoclonal antibodies on hydrazide or amino Eupergit C derivatives thus leads to the formation of antibody matrix conjugates which possess high antigen-binding activities.

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Citations

Jul 17, 2012·Analytical and Bioanalytical Chemistry·Dilip ShresthaAttila Jenei
Mar 27, 1995·Journal of Immunological Methods·E RonB Solomon
May 16, 2002·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Zuzana BílkováJaroslav Churácek
Mar 6, 1999·Journal of Chromatography. B, Biomedical Sciences and Applications·J Turková
May 10, 2002·Journal of Biotechnology·K Busch, R Tampé
May 28, 2003·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Vladimir I Muronetz, Timo Korpela
Aug 6, 2013·Biosensors & Bioelectronics·Asta Makaraviciute, Almira Ramanaviciene
Apr 24, 1992·Journal of Chromatography·J TurkováM Tichá

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