Structure and immunomodulation activity of a novel mannose binding lectin from housefly pupae / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 601-611, 2013.
Artículo
en Chino
| WPRIM
| ID: wpr-233217
ABSTRACT
We purified a novel mannose binding lectin form Musca domestica pupae by affinity chromatography on Con A-Sepharose 4B and DEAE weak anion-exchange chromatography. By SDS-PAGE, MBL-1 yielded a single band with the molecular weight of 24 kDa. It was a glycoprotein detected by periodic acid-schiffs staining reaction, with 97.36% protein and 2.1% oligosaccharide. Meanwhile, the results of beta-elimination reaction, infrared spectroscopy, atomic force microscopy and protein sequencing instrument show that MBL-1 was an ellipsoidal-shaped monomer with 60-100 nm in diameter. N-glycoside bond linked oligosaccharide chain and the N-terminal blocked peptide chain. Further study suggested that MBL-1 promote the proliferation of macrophage in a concentration-dependent manner. The scanning electron microscope analysis shows that MBL-1 promoted the activation of macrophages. These results show that MBL-1 purified from Musca domestica pupae possesses immune regulation effect, serving a reference basis to develop natural immune-modulator.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Oligosacáridos
/
Fisiología
/
Pupa
/
Glicoproteínas
/
Química
/
Lectina de Unión a Manosa
/
Alergia e Inmunología
/
Inmunomodulación
/
Moscas Domésticas
/
Macrófagos
Límite:
Animales
Idioma:
Chino
Revista:
Chinese Journal of Biotechnology
Año:
2013
Tipo del documento:
Artículo
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