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.

Metadaten
Verfasserangaben:	Katrin Messerschmidt ORCiD GND, Janine Degen, Burkhard Micheel
DOI:	https://doi.org/10.1002/jmr.1136
ISSN:	0952-3499
Titel des übergeordneten Werks (Englisch):	Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine
Verlag:	Wiley-Blackwell
Verlagsort:	Malden
Publikationstyp:	Wissenschaftlicher Artikel
Sprache:	Englisch
Jahr der Erstveröffentlichung:	2011
Erscheinungsjahr:	2011
Datum der Freischaltung:	26.03.2017
Freies Schlagwort / Tag:	catalytic antibody; fluorescein; oxidoreductase; resazurin; resorufin
Band:	24
Ausgabe:	6
Seitenanzahl:	5
Erste Seite:	930
Letzte Seite:	934
Fördernde Institution:	International Max Planck Research School on Biomimetic Systems; Max Planck Society; State of Brandenburg
Organisationseinheiten:	Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:	Referiert