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Biotechnol Appl Biochem. 1997 Oct;26(2):103-9.

Conjugation of catalase to a carrier antibody via a streptavidin-biotin cross-linker.

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Institute for Environmental Medicine, University of Pennsylvania Medical School, Philadelphia, USA.


Targeting of catalase could be useful in antioxidative protection of cells challenged with H2O2. In the present study we conjugated catalase to a carrier model antibody using a biotin-streptavidin (SA) cross-linker and characterized the functional activity of the conjugate. Neither biotinylation nor conjugation with SA decreased the enzymic activity of catalase. Further coupling of radiolabelled biotinylated catalase (b-catalase) to biotinylated antibody (b-Ab) via SA using a two-step conjugation procedure did not change enzymic activity of b-catalase. b-Ab-SA-b-catalase specifically bound to antigen-coated plastic wells, but not to albumin-coated plastic wells. Substitution of b-Ab with control biotinylated IgG (b-IgG) abrogated binding of the catalase to the antigen. H2O2 was degraded in antigen-coated wells preincubated with b-Ab-SA-b-catalase, but not with b-IgG-SA-b-catalase. Thus b-Ab-SA-b-catalase specifically binds to immobilized antigen and degrades H2O2 after binding to the target. The methodology described in the present paper may be useful for the development of a novel strategy for antioxidant therapy.

[Indexed for MEDLINE]

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