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外文期刊>The biochemical journal
>Immunoaffinity purification of avermectin-binding proteins from the free-living nematode Caenorhabditis elegans and the fruitfly Drosophila melanogaster
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Immunoaffinity purification of avermectin-binding proteins from the free-living nematode Caenorhabditis elegans and the fruitfly Drosophila melanogaster
pAvermectin-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./p
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