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

Beka Solomon, Rela Koppel, Fidi Schwartz, Gideon Fleminger

Research output: Contribution to journalArticlepeer-review

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 selectivity 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.

Original languageEnglish
Pages (from-to)321-329
Number of pages9
JournalJournal of Chromatography A
Volume510
Issue numberC
DOIs
StatePublished - 27 Jun 1990

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