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
in Zh
| WPRIM
| ID: wpr-249984
Responsible library:
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.
Full text:
1
Index:
WPRIM
Main subject:
Pharmacology
/
Bacterial Toxins
/
Recombinant Fusion Proteins
/
Immunoglobulin Fragments
/
Carcinoembryonic Antigen
/
Immunotoxins
/
Cloning, Molecular
/
ADP Ribose Transferases
/
Protein Renaturation
/
Virulence Factors
Limits:
Humans
Language:
Zh
Journal:
Chinese Journal of Biotechnology
Year:
2004
Type:
Article