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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.
Author details: | Katrin MesserschmidtORCiDGND, Janine Degen, Burkhard Micheel |
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DOI: | https://doi.org/10.1002/jmr.1136 |
ISSN: | 0952-3499 |
Title of parent work (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 publishing: | Malden |
Publication type: | Article |
Language: | English |
Year of first publication: | 2011 |
Publication year: | 2011 |
Release date: | 2017/03/26 |
Tag: | catalytic antibody; fluorescein; oxidoreductase; resazurin; resorufin |
Volume: | 24 |
Issue: | 6 |
Number of pages: | 5 |
First page: | 930 |
Last Page: | 934 |
Funding institution: | 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 |