Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes
The Korean Journal of Parasitology
; : 157-160, 2005.
Article
en En
| WPRIM
| ID: wpr-215234
Biblioteca responsable:
WPRO
ABSTRACT
A 29 kDa cysteine protease of Taenia solium metacestodes was purified by Mono Q anion-exchanger and Superose 6 HR gel filtration chromatography. The enzyme was effectively inhibited by cysteine protease inhibitors, such as iodoacetic acid (IAA) and trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) while inhibitors acting on serine- or metallo-proteases did not affect the enzyme activity. The purified enzyme degraded human immunoglobulin G (IgG), collagen and bovine serum albumin (BSA), but human IgG was more susceptible for proteolysis by the enzyme. To define the precise biological roles of the enzyme, more detailed biochemical and functional studies would be required.
Palabras clave
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Inmunoglobulina G
/
Albúmina Sérica Bovina
/
Cisteína Endopeptidasas
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Inhibidores de Cisteína Proteinasa
/
Cromatografía en Gel
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Cromatografía por Intercambio Iónico
/
Colágeno
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Ácido Yodoacético
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Taenia solium
/
Leucina
Límite:
Animals
/
Humans
Idioma:
En
Revista:
The Korean Journal of Parasitology
Año:
2005
Tipo del documento:
Article