Highly active enzyme preparations immobilized via matrix-conjugated anti-Fc antibodies

Beka Solomon*, Eran Hadas, Rela Koppel, Fidi Schwartz, Gideon Fleminger

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


A novel method for enzyme immobilization to achieve highly active enzyme preparations is described. The enzyme is first reacted in solution with a specific monoclonal antibody (mAb) which does not interfere with its enzymic activity and which possesses a high affinity towards the enzyme, The immunocomplex is then reacted with immobilized anti-Fc antibodies which are coupled to the matrix by methods that preserve maximum immunological activity. Horseradish peroxidase (HRP) immobilization on epoxy-activated beads (CB6200) was chosen as a model system for this approach. Coupling of HRP via its mAbs to anti-Fc antibodies immobilized yielded the best results, corresponding to binding of 325 ng of fully active enzyme per bead. Binding of the enzyme to anti-HRP mAb directly immobilized on the beads was considerably lower.

Original languageEnglish
Pages (from-to)335-341
Number of pages7
JournalJournal of Chromatography A
Issue number2
StatePublished - 1991


Dive into the research topics of 'Highly active enzyme preparations immobilized via matrix-conjugated anti-Fc antibodies'. Together they form a unique fingerprint.

Cite this