Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes
The Korean Journal of Parasitology
; : 157-160, 2005.
Article
em En
| WPRIM
| ID: wpr-215234
Biblioteca responsável:
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.
Palavras-chave
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Imunoglobulina G
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Soroalbumina Bovina
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Cisteína Endopeptidases
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Inibidores de Cisteína Proteinase
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Cromatografia em Gel
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Cromatografia por Troca Iônica
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Colágeno
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Ácido Iodoacético
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Taenia solium
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Leucina
Limite:
Animals
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Humans
Idioma:
En
Revista:
The Korean Journal of Parasitology
Ano de publicação:
2005
Tipo de documento:
Article