Partial Purification and Properties of a Cysteine Protease from Citrus Red Mite Panonychus citri
The Korean Journal of Parasitology
;
: 117-120, 2014.
Artigo
em Inglês
| WPRIM
| ID: wpr-14498
ABSTRACT
Several studies have reported that the citrus red mites Panonychus citri were an important allergen of citrus-cultivating farmers in Jeju Island. The aim of the present study was to purify and assess properties of a cysteine protease from the mites acting as a potentially pathogenic factor to citrus-cultivating farmers. A cysteine protease was purified using column chromatography of Mono Q anion exchanger and Superdex 200 HR gel filtration. It was estimated to be 46 kDa by gel filtration column chromatography and consisted of 2 polypeptides, at least. Cysteine protease inhibitors, such as trans poxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) and iodoacetic acid (IAA) totally inhibited the enzyme activities, whereas serine or metalloprotease inhibitors did not affect the activities. In addition, the purified enzyme degraded human IgG, collagen, and fibronectin, but not egg albumin. From these results, the cysteine protease of the mites might be involved in the pathogenesis such as tissue destruction and penetration instead of nutrient digestion.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Especificidade por Substrato
/
Imunoglobulina G
/
Inibidores de Cisteína Proteinase
/
Cromatografia em Gel
/
Cromatografia por Troca Iônica
/
Colágeno
/
Fibronectinas
/
Subunidades Proteicas
/
Tetranychidae
/
Cisteína Proteases
Limite:
Animais
/
Humanos
Idioma:
Inglês
Revista:
The Korean Journal of Parasitology
Ano de publicação:
2014
Tipo de documento:
Artigo
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