Production and tumour-binding characterization of a chimeric anti-CEA Fab expressed inEschericwa coli
| Autor: | Robert E. Hawkins, P. A. Keep, KA Chester, Richard H. J. Begent, RB Pedley, J. A. Boden, Lisa Robson, GM Boxer |
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| Rok vydání: | 1994 |
| Předmět: |
Cancer Research
medicine.drug_class Recombinant Fusion Proteins Molecular Sequence Data Transplantation Heterologous Immunocytochemistry Immunoglobulin Variable Region Gene Expression Adenocarcinoma Monoclonal antibody medicine.disease_cause law.invention Mice Carcinoembryonic antigen Affinity chromatography law Escherichia coli medicine Animals Humans Tissue Distribution Amino Acid Sequence Cloning Molecular Immunoglobulin Fragments Base Sequence biology Molecular biology Carcinoembryonic Antigen Oncology Monoclonal biology.protein Recombinant DNA Antibody Colorectal Neoplasms Immunoglobulin Constant Regions |
| Zdroj: | International Journal of Cancer. 57:67-72 |
| ISSN: | 1097-0215 0020-7136 |
| Popis: | A recombinant chimeric Fab (rcFab), with Fv derived from the monoclonal A5B7 antibody to carcinoembryonic antigen (CEA), and with human CHI and C kappa was cloned into pUC 19 and expressed in Escherichia coli. rcFab (10 to 12 mg per litre) was produced in bacterial culture fluid, and functional purified rcFab was isolated by affinity chromatography (using antibody to human C kappa) and size-exclusion gel filtration. The rcFab did not show reduced affinity for CEA, and reacted with human colorectal tumours showing a typical anti-CEA pattern by immunocytochemistry; it was also stable after iodination. Biodistribution studies in nude mice bearing human tumour xenografts showed no toxicity and good tumour localization. Therapeutic ratios at early time points were better than those obtained with whole murine antibody. The results demonstrate that bacterially produced anti-CEA Fab is of use for tumour targeting. |
| Databáze: | OpenAIRE |
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