| Autor: |
Rohrer, S P, Jacobson, E B, Hayes, E C, Birzin, E T, Schaeffer, J M |
| Zdroj: |
Biochemical Journal; September 1994, Vol. 302 Issue: 2 p339-345, 7p |
| Abstrakt: |
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: |
Supplemental Index |
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