Over-expression of the yeast ATP synthase subunit D in Escherichia coli: use of polyclonal antibodies directed against recombinant subunit D
| Autor: | J. Vaillier, Jean Velours, N. Norais |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Protein Conformation
Protein subunit Saccharomyces cerevisiae Genes Fungal Molecular Sequence Data Biophysics DNA Recombinant Gene Expression Biology medicine.disease_cause Biochemistry Gamma-aminobutyric acid receptor subunit alpha-1 Interleukin 10 receptor alpha subunit Multienzyme Complexes medicine Escherichia coli Molecular Biology Antibodies Fungal ATP synthase Base Sequence Wild type Cell Biology biology.organism_classification Molecular biology Recombinant Proteins Proton-Translocating ATPases Polyclonal antibodies biology.protein |
| Zdroj: | Biochemical and biophysical research communications. 200(2) |
| ISSN: | 0006-291X |
| Popis: | The yeast ATP synthase subunit d was over-expressed in E. coli and formed inclusion bodies. It was purified by solubilization in urea and slow removal of the urea by stepwise dialysis in the presence of a non-ionic detergent. The resulting soluble subunit d was used to prepare polyclonal antibodies. Blots of yeast mitochondrial proteins were probed with these antibodies. The strain disrupted in ATP4 gene encoding the subunit 4 displayed only 8% of the wild type subunit d. Antibodies against subunit d did not inhibit the wild type ATPase activity. |
| Databáze: | OpenAIRE |
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