An Fv catalytic antibody with high glutathione peroxidase (GPX) activity wa
s prepared using proteolysis of a monoclonal antibody 3H4 (IgM), and subseq
uent chemical mutation. The Fv fragment generated by pepsin digestion of 3H
4 retained binding activity for glutathione (GSH), one substrate of GPX. Ac
tive serines in the binding site of the Fv fragment were converted to selen
ocysteine, the catalytic group of GPX. The selenium-containing Fv fragment
exhibits a high GPX activity of the same order of magnitude as native GPX f
rom rabbit liver. (C) 1999 Elsevier Science S.A. All rights reserved.