Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation
The Korean Journal of Parasitology
;
: 57-60, 2004.
Artigo
em Inglês
| WPRIM
| ID: wpr-188037
ABSTRACT
A highly specific antigenic protein of 31 kDa from plerocercoid of Spirometra mansoni (sparganum) was obtained by gelatin affinity and Mono Q anion-exchange column chromatography. The purified 31 kDa protein was subjected to N-glycan enzymatic digestion for structural analysis. The relative electrophoretic mobility was analyzed by SDS-PAGE, before and after digestion. On SDS-PAGE after enzymatic digestion, the 31 kDa protein showed a molecular shift of approximately 2 kDa, which indicated the possession of complex N-linked oligosaccharides (N-glycosidase F sensitive) but not of high-mannose oligosaccharides (endo-beta-N-acetylglucosaminidase H, non-sensitive). Chemically periodated 31 kDa protein showed statistically non-significant changes with human sparganosis sera by enzyme linked immunosorbent assay (ELISA). Therefore, the dominant epitopes of the 31 kDa molecule in human sparganosis were found to be mainly polypeptide, while N-glycans of the antigenic molecule in sparganum was minimal in anti-carbohydrate antibody production.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Plerocercoide
/
Spirometra
/
Ensaio de Imunoadsorção Enzimática
/
Carboidratos
/
Esparganose
/
Cromatografia de Afinidade
/
Cromatografia por Troca Iônica
/
Ácido Periódico
/
Eletroforese em Gel de Poliacrilamida
/
Hexosaminidases
Limite:
Animais
/
Humanos
Idioma:
Inglês
Revista:
The Korean Journal of Parasitology
Ano de publicação:
2004
Tipo de documento:
Artigo
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