• Treffer 3 von 0
Zurück zur Trefferliste

Enzyme activity determination of human monoamine oxidase B (Mao B) by amperometric hydrogen peroxide detection

  • Parkinson’s disease (PD) is one of the most common neurodegenerative disorders worldwide. About 0.3 % of the global population and approximately 2 % of people older than 80 years are affected by PD. Monoamine oxidase B (Mao B) is an enzyme, which is a drug target in Parkinson’s disease (PD), since it is involved in dopamine metabolism. Several Mao B inhibitors are well established as medication for PD patients. However, the medical treatment is only little personalized since the monitoring of the patients Mao B activity is complex and requires sophisticated laboratory equipment. Here a sensorial Mao B activity determination system has been developed which has potential in the personalization of the medical PD treatment. The enzyme activity is quantified by amperometric detection of enzymatically produced H2O2. Therefore, the enzyme is enriched from the solution via cellulose particles which are functionalized with antibodies against human Mao B. The successful capturing of the enzymeParkinson’s disease (PD) is one of the most common neurodegenerative disorders worldwide. About 0.3 % of the global population and approximately 2 % of people older than 80 years are affected by PD. Monoamine oxidase B (Mao B) is an enzyme, which is a drug target in Parkinson’s disease (PD), since it is involved in dopamine metabolism. Several Mao B inhibitors are well established as medication for PD patients. However, the medical treatment is only little personalized since the monitoring of the patients Mao B activity is complex and requires sophisticated laboratory equipment. Here a sensorial Mao B activity determination system has been developed which has potential in the personalization of the medical PD treatment. The enzyme activity is quantified by amperometric detection of enzymatically produced H2O2. Therefore, the enzyme is enriched from the solution via cellulose particles which are functionalized with antibodies against human Mao B. The successful capturing of the enzyme can be verified by SDS-PAGE. For activity determination the enzyme is brought in contact with a suitable substrate - here benzylamine. Selectivity of the amperometric hydrogen peroxide detection in the presence of co-reactants has been verified. Within the time span of 30 min, a linear dependency of enzymatically produced H2O2 with the substrate incubation time can be observed. This allows the evaluation of the Mao B activity. The results have been correlated to an optical detection method. Furthermore, the method has been tested for different amounts of enzyme used in the experiments and found to be sensitive enough for Mao B analysis in blood samples.zeige mehrzeige weniger

Volltext Dateien herunterladen

  • EBS Mao B - Soraya Hoefs.pdf
    eng
  • ebs_Hoefs_MaoB.pdf
    eng

Metadaten exportieren

Weitere Dienste

Teilen auf Twitter Suche bei Google Scholar Anzahl der Zugriffe auf dieses Dokument
Metadaten
Autor*innen:Soraya RiedelORCiD
Koautor*innen:A. Talke, F. Lisdat
Dokumenttyp:Vortrag
Veröffentlichungsform:Präsentation
Sprache:Englisch
Jahr der Erstveröffentlichung:2021
Organisationseinheit der BAM:1 Analytische Chemie; Referenzmaterialien
1 Analytische Chemie; Referenzmaterialien / 1.8 Umweltanalytik
DDC-Klassifikation:Naturwissenschaften und Mathematik / Chemie / Analytische Chemie
Freie Schlagwörter:Amperometry; Monoamine oxidase B; Parkinsons's disease; Prussian blue; Screen-printed electrodes
Themenfelder/Aktivitätsfelder der BAM:Chemie und Prozesstechnik
Chemie und Prozesstechnik / Chemische Charakterisierung und Spurenanalytik
Veranstaltung:European Biosensor Symposium 2021
Veranstaltungsort:Online meeting
Beginndatum der Veranstaltung:09.03.2021
Enddatum der Veranstaltung:12.03.2021
Bemerkung:
Geburtsname von Riedel, Soraya: Höfs, S. -  Birth name of Riedel, Soraya: Höfs, S.
Verfügbarkeit des Dokuments:Datei im Netzwerk der BAM verfügbar ("Closed Access")
Datum der Freischaltung:15.03.2021
Referierte Publikation:Nein
Eingeladener Vortrag:Nein
Einverstanden
Diese Webseite verwendet technisch erforderliche Session-Cookies. Durch die weitere Nutzung der Webseite stimmen Sie diesem zu. Unsere Datenschutzerklärung finden Sie hier.