Characterisation of two soluble metalloexopeptidases in the protozoan parasite Leishmania major.

Détails

ID Serval
serval:BIB_8A0081AB1957
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Characterisation of two soluble metalloexopeptidases in the protozoan parasite Leishmania major.
Périodique
Molecular and Biochemical Parasitology
Auteur⸱e⸱s
Schneider P., Glaser T.A.
ISSN
0166-6851 (Print)
ISSN-L
0166-6851
Statut éditorial
Publié
Date de publication
1993
Volume
62
Numéro
2
Pages
223-231
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Two soluble exopeptidases were identified in promastigotes of Leishmania major, using an iodinated model tetrapeptide (LIAY) as substrate. Similar activities were also detected in L. major amastigotes and in different species of Leishmania promastigotes. A carboxy- and an aminopeptidase activity were resolved and isolated by anion exchange and gel permeation chromatographies. A single polypeptide of 62 kDa co-purified with the aminopeptidase activity. Optimum pH was neutral for the carboxypeptidase and neutral to alkaline for the aminopeptidase. Both activities were able to hydrolyse a dipeptide substrate (YL), and were inhibited by 20 microM bestatin and 200 microM 1,10-phenanthroline, but not by leupeptin, iodoacetamide and a range of other inhibitors. These results strongly suggest that both enzymes are metalloexopeptidases and thus represent a novel class of soluble peptidases in Leishmania.
Mots-clé
Amino Acid Sequence, Animals, Chromatography, Gel, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Leishmania major/enzymology, Leishmaniasis/parasitology, Metalloendopeptidases/antagonists & inhibitors, Metalloendopeptidases/isolation & purification, Mice, Molecular Sequence Data, Peptides, Solubility, Substrate Specificity
Pubmed
Web of science
Création de la notice
19/01/2008 18:30
Dernière modification de la notice
20/08/2019 15:48
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