Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe.
Biol Chem
; 386(4): 401-6, 2005 Apr.
Article
em En
| MEDLINE
| ID: mdl-15899703
ABSTRACT
Trophozoite cysteine protease (TCP) activity, isolated from Plasmodium falciparum soluble 100,000 g extracts, displayed native falcipain-1 kinetic parameters towards peptidyl substrates. The labelling of either isolated TCP or soluble 100,000 g extracts by a cystatin-derived probe (biotinyl-Leu-Val-Gly-CHN2) revealed a single band of ca. 30 kDa by SDS-PAGE, which was resolved into four spots displaying isoelectric points (pI) from 4.7 to 5.3 after two-dimensional separation. The molecular mass and pI correspond to those of falcipain-3, falcipain-2, falcipain-2' and falcipain-1, respectively. The two central spots were identified by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry as falcipain-2 and falcipain-2'. This activity-based probe represents a potential tool for profiling active falcipains in parasites.
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Base de dados:
MEDLINE
Assunto principal:
Plasmodium falciparum
/
Cisteína Endopeptidases
/
Sondas Moleculares
/
Cistatinas
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article