Immunoaffinity purification of avermectin-binding proteins from the free-living nematode Caenorhabditis elegans and the fruitfly Drosophila melanogaster
| Autor: | Susan P. Rohrer, James M. Schaeffer, Elizabeth T. Birzin, E B Jacobson, Edward C. Hayes |
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| Rok vydání: | 1994 |
| Předmět: |
Biochemistry
DNA-binding protein Chromatography Affinity Affinity chromatography Animals Caenorhabditis elegans Molecular Biology Polyacrylamide gel electrophoresis Ivermectin biology Binding protein Antibodies Monoclonal Cell Biology biology.organism_classification Precipitin Tests Molecular biology Drosophila melanogaster Electroelution Chromatography Gel Electrophoresis Polyacrylamide Gel Carrier Proteins Drosophila Protein Research Article |
| Zdroj: | Biochemical Journal. 302:339-345 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3020339 |
| Popis: | Avermectin-binding proteins from the free-living nematode worm Caenorhabditis elegans and from the fruitfly Drosophila melanogaster were purified to homogeneity via a three-step procedure. The binding proteins were covalently labelled using a radioactive photoaffinity probe and then partially purified on a Sephacryl S-300 gel-filtration column. The radiolabelled binding proteins were then purified by immunoaffinity chromatography using a monoclonal antibody to avermectin covalently attached to Protein A-Sepharose beads. Three affinity-labelled Drosophila proteins with molecular masses between 45 and 50 kDa were isolated in this way and then separated from each other by electroelution. This three-step protocol provides a rapid technique for receptor purification which may be of use in the purification of other binding proteins. |
| Databáze: | OpenAIRE |
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