Fast purification of Clostridium sordellii cytotoxin
| Autor: | Gaynor A. Green, Henri Monteil, Raymonde Girardot, Bertrand H. Rihn, Olivier Baldacini |
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| Rok vydání: | 1990 |
| Předmět: |
Titration curve
Protein Conformation Sodium Protein subunit Bacterial Toxins Immunoblotting chemistry.chemical_element Ultrafiltration Clostridium sordellii medicine.disease_cause Bacterial Proteins medicine Amino Acids Cytotoxicity Polyacrylamide gel electrophoresis Clostridium Antigens Bacterial Chromatography biology Staining and Labeling Chemistry Toxin General Chemistry biology.organism_classification Chromatography Ion Exchange Biochemistry Polyclonal antibodies biology.protein Electrophoresis Polyacrylamide Gel Isoelectric Focusing |
| Zdroj: | Journal of chromatography. 528(2) |
| Popis: | We have developed a rapid method for the purification of proteins, combining titration curve analysis with a two-step column chromatographic procedure. We have used this approach to purify the cytotoxin (L toxin) from Clostridium sordellii . We have also determined the amino acid composition of this cytotoxin. This toxin has a p I value of 4.20 and an M r of 260 000, reduction of which results in a band of M r 43 000 on sodium dodecyl sulphate polyacrylamide gel electrophoresis. Since both the proteins of M r 260 000 and 43 000 are recognized by the polyclonal anti- C. sordellii L toxin, which neutralizes the L toxin cytotoxicity, we propose a hexameric structure for the protein of M r 260 000, each subunit being M r 43 000. |
| Databáze: | OpenAIRE |
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