UNIGE document Scientific Article
previous document  unige:10616  next document
add to browser collection
Title

Human recombinant monoamine oxidase B as reliable and efficient enzyme source for inhibitor screening

Authors
Novaroli, L.
Reist, Marianne
Favre, Elisabeth
Carotti, Angelo
Catto, M.
Published in Bioorganic & Medicinal Chemistry. 2005, vol. 13, no. 22, p. 6212-6217
Abstract Interest in inhibitors of monoamine oxidase type B (MAO B) has grown in recent years, due to their therapeutic potential in aging-related neurodegenerative diseases, such as Parkinson's disease and Alzheimer's disease. This study is devoted to the use of human recombinant MAO B obtained from a Baculovirus expression system (Supersomes MAO B, BD Gentest, MA, USA) as reliable and efficient enzyme source for MAO B inhibitor screening. Comparison of inhibition potencies (pIC50 values) determined with human cloned and human platelet MAO B for the two series of MAO B inhibitors, coumarin and 5H-indeno[1,2-c]pyridazin-5-one derivatives, showed that the difference between pIC50 values obtained with the two enzyme sources was not significant (P>0.05, Student's t-test). Hence, recombinant enzyme is validated as convenient enzyme source for MAO B inhibitor screening.
Keywords Blood Platelets/drug effects/enzymologyCoumarins/analysis/chemistry/pharmacologyDrug Evaluation, Preclinical/methodsHumansInhibitory Concentration 50Monoamine Oxidase/*drug effects/*genetics/metabolismMonoamine Oxidase Inhibitors/analysis/chemistry/*pharmacologyPyridazines/analysis/classification/pharmacologyRecombinant Proteins/*genetics
Identifiers
PMID: 16054369
Full text
Structures
Citation
(ISO format)
NOVAROLI, L. et al. Human recombinant monoamine oxidase B as reliable and efficient enzyme source for inhibitor screening. In: Bioorganic & Medicinal Chemistry, 2005, vol. 13, n° 22, p. 6212-6217. https://archive-ouverte.unige.ch/unige:10616

118 hits

0 download

Update

Deposited on : 2010-08-06

Export document
Format :
Citation style :