Biochemical characterization and assessment of leishmanicidal effects of a new L-amino acid oxidase from Crotalus durissus collilineatus snake venom (CollinLA AO-I).
L-amino acid Oxidase
Leishmania spp.
Leishmanicidal activity
ROS
Snake venom
Journal
Toxicon : official journal of the International Society on Toxinology
ISSN: 1879-3150
Titre abrégé: Toxicon
Pays: England
ID NLM: 1307333
Informations de publication
Date de publication:
Jul 2023
Jul 2023
Historique:
received:
13
01
2023
revised:
04
05
2023
accepted:
08
05
2023
medline:
14
6
2023
pubmed:
12
5
2023
entrez:
11
5
2023
Statut:
ppublish
Résumé
This study reports the isolation of CollinLAAO-I, a new L-amino acid oxidase from Crotalus durissus collilineatus snake venom, its biochemical characterization and leishmanicidal potential in Leishmania spp. CollinLAAO-I (63.1 kDa) was successfully isolated with high purity using two chromatographic steps and represents 2.5% of total venom proteins. CollinLAAO-I displayed high enzymatic activity (4262.83 U/mg/min), significantly reducing after 28 days. The enzymatic activity of CollinLAAO-I revealed higher affinity for hydrophobic amino acids such as L-leucine, high enzymatic activity in a wide pH range (6.0-10.0), at temperatures from 0 to 25 °C, and showed complete inhibition in the presence of Na
Identifiants
pubmed: 37169266
pii: S0041-0101(23)00142-3
doi: 10.1016/j.toxicon.2023.107156
pii:
doi:
Substances chimiques
L-Amino Acid Oxidase
EC 1.4.3.2
Crotalid Venoms
0
Snake Venoms
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
107156Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.