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Oxidoreductase activity of multifunctional monoclonal antibody B13-DE1

  • The monoclonal antibody B13-DE1 binds fluorescein, several fluorescein derivatives, and three peptide mimotopes. Our results revealed that this antibody also catalyzed the redox reaction of resazurin to resorufin, which are both structurally related to fluorescein. By using sodium sulfite as a reducing agent, the antibody B13-DE1 lowered the activation energy of this reaction. The Michaelis-Menten constant and turnover number of the catalyzed reaction were determined as 4.2 mu mol/l and 0.0056 s(-1), respectively. Because the results showed that fluorescein inhibited the catalytic activity of the antibody, we assume that the antigen-binding site and the catalytic active site are identical.

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Metadaten
Author:Katrin Messerschmidt, Janine Degen, Burkhard Micheel
DOI:https://doi.org/10.1002/jmr.1136
ISSN:0952-3499 (print)
Parent Title (English):Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine
Publisher:Wiley-Blackwell
Place of publication:Malden
Document Type:Article
Language:English
Year of first Publication:2011
Year of Completion:2011
Release Date:2017/03/26
Tag:catalytic antibody; fluorescein; oxidoreductase; resazurin; resorufin
Volume:24
Issue:6
Pagenumber:5
First Page:930
Last Page:934
Funder:International Max Planck Research School on Biomimetic Systems; Max Planck Society; State of Brandenburg
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert