Molecular and functional characterisation of a fusion protein suited for tumour specific prodrug activation
| Autor: | J Czech, G. Seemann, M Schuermann, K. Bosslet, H.H. Sedlacek, P. Lorenz |
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| Jazyk: | angličtina |
| Rok vydání: | 1992 |
| Předmět: |
Cancer Research
medicine.drug_class Recombinant Fusion Proteins Monoclonal antibody Transfection Immunoglobulin G law.invention Cell Line Affinity chromatography law medicine Avidity Prodrugs Promoter Regions Genetic biology Prodrug Hydrogen-Ion Concentration Molecular biology Fusion protein Carcinoembryonic Antigen A-site Oncology Biochemistry biology.protein Recombinant DNA Genetic Engineering Research Article |
| Zdroj: | British Journal of Cancer |
| ISSN: | 1532-1827 0007-0920 |
| Popis: | A fusion protein consisting of the humanised Fab fragment of the anti CEA MAb BW 431 and the human beta-glucuronidase was expressed in BHK cells. Functional testing revealed that the specificity and avidity of the humanised V region was similar to the original murine MAb BW 431. Furthermore, the enzymatic activity, pH sensitivity and stability of the human beta-glucuronidase in the fusion protein was comparable to the activity of recombinant human beta-glucuronidase. Using anti-idiotype affinity chromatography, two molecules of a molecular weight of 125 kDa or 250 kDa could be visualized under nonreducing conditions in SDS-PAGE. Reducing conditions revealed a 25 kDa light and 100 kDa heavy chain. Due to its suitable biological characteristics this fusion protein might be an appropriate molecule allowing a site specific antibody directed enzyme prodrug therapy (ADEPT) in vivo. Images Figure 1 |
| Databáze: | OpenAIRE |
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