Oxidoreductase activity of multifunctional monoclonal antibody B13-DE1.
Summary of "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 µmol/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. Copyright © 2011 John Wiley & Sons, Ltd.
Affiliation
Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht Strasse 24-25, 14476, Golm, Germany. katrin.messerschmidt@uni-potsdam.de.
Journal Details
This article was published in the following journal.
Name: Journal of molecular recognition : JMR
ISSN: 1099-1352
Pages: 930-4
Links
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/22038799
- DOI: http://dx.doi.org/10.1002/jmr.1136
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