Studies of the expression, purification, renaturation and biologic activity of an anti-CEA immunotoxin / 生物工程学报
Chinese Journal of Biotechnology
; (12): 348-351, 2004.
Article
de Zh
| WPRIM
| ID: wpr-249984
Bibliothèque responsable:
WPRO
ABSTRACT
A recombinant immunotoxin named CEA/PE38/KDEL was constructed, which was composed of anti-CEA single-chain Fv and the truncated and modified form of Pseudomonas exotoxin (PE38/KDEL). The CEA/PE38/KDEL immunotoxin was expressed in the E. coli strain BL21 (DE3)-star as inclusion bodies. The denatured inclusion bodies were purified with Ni-NTA chelate agarose, then the constant gradient dialysis was used to perform the refolding of the CEA/PE38/KDEL immunotoxin. Results of FACS and MTT assay indicate that the refolded immunotoxins keep potent and specific cytotoxicity to tumor cells bearing CEA antigens.
Texte intégral:
1
Indice:
WPRIM
Sujet Principal:
Pharmacologie
/
Toxines bactériennes
/
Protéines de fusion recombinantes
/
Fragments d'immunoglobuline
/
Antigène carcinoembryonnaire
/
Immunotoxines
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Clonage moléculaire
/
ADP ribose transferases
/
Renaturation des protéines
/
Facteurs de virulence
Limites du sujet:
Humans
langue:
Zh
Texte intégral:
Chinese Journal of Biotechnology
Année:
2004
Type:
Article