| Autor: |
Imanaka Tadayuki, Tsukio Manae, Tungpradabkul Sumalee, Sandee Duanpen, Takagi Masahiro |
| Jazyk: |
angličtina |
| Rok vydání: |
2002 |
| Předmět: |
|
| Zdroj: |
BMC Biotechnology, Vol 2, Iss 1, p 16 (2002) |
| Druh dokumentu: |
article |
| ISSN: |
1472-6750 |
| DOI: |
10.1186/1472-6750-2-16 |
| Popis: |
Abstract Background Hep27 monoclonal (Hep27 Mab) is an antibody against hepatocellular carcinoma. Hep27 Mab itself can inhibit the growth of a hepatocellular carcinoma cell line (HCC-S102). We attempted to produce a single-chain fragment (scFv), a small fragment containing an antigen-binding site of Hep27 Mab, by using DNA-recombinant techniques. Results The sequences encoding the variable regions of heavy (VH) and light (VL) chains of a murine Hep27 Mab were linked together by a linker peptide (Gly4Ser)3 and tagged with a hexa-histidine at the C-terminal; the resultant DNA construct was expressed in E. coli as an insoluble protein. The denatured scFv was refolded and purified by immobilized metal ion affinity chromatography (12 mg/l with a molecular weight of 27 kDa). Hep27scFv exhibited a tumoricidal activity against the HCC-S102 cell as its parental antibody (Hep27 Mab). Conclusion This scFv may be a potential candidate for a targeting agent in HCC immunodiagnosis or immunotherapy. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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