A New Activity Assay Method for Diamine Oxidase Based on Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry.
MALDI
activity assay
amine oxidase
enzyme kinetics
polyamine
reaction rate
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
14 Oct 2024
14 Oct 2024
Historique:
received:
13
09
2024
revised:
08
10
2024
accepted:
10
10
2024
medline:
26
10
2024
pubmed:
26
10
2024
entrez:
26
10
2024
Statut:
epublish
Résumé
Copper-containing diamine oxidases are ubiquitous enzymes that participate in many important biological processes. These processes include the regulation of cell growth and division, programmed cell death, and responses to environmental stressors. Natural substrates include, for example, putrescine, spermidine, and histamine. Enzymatic activity is typically assayed using spectrophotometric, electrochemical, or fluorometric methods. The aim of this study was to develop a method for measuring activity using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry based on the intensity ratio of product to product-plus-substrate signals in the reaction mixtures. For this purpose, an enzyme purified to homogeneity from pea (
Identifiants
pubmed: 39459245
pii: molecules29204878
doi: 10.3390/molecules29204878
pii:
doi:
Substances chimiques
Amine Oxidase (Copper-Containing)
EC 1.4.3.21
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Palacký University Olomouc
ID : IGA_PrF_2022_025
Déclaration de conflit d'intérêts
The authors declare no conflicts of interest.