Idioma:

Fast purification of Clostridium sordellii cytotoxin

Baldacini, Olivier ; Green, Gaynor A. ; Girardot, Raymonde ; Rihn, Bertrand ; Monteil, Henri

Journal of chromatography, 1990, Vol.528 (2), p.357-369

Texto completo disponível

Citações Citado por

Título:
Fast purification of Clostridium sordellii cytotoxin
Autor: Baldacini, Olivier ; Green, Gaynor A. ; Girardot, Raymonde ; Rihn, Bertrand ; Monteil, Henri
Assuntos: Amino Acids - analysis ; Antigens, Bacterial - isolation & purification ; Bacterial Proteins - isolation & purification ; Bacterial Toxins - immunology ; Bacterial Toxins - isolation & purification ; Chromatography, Ion Exchange ; Clostridium - analysis ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Isoelectric Focusing ; Protein Conformation ; Staining and Labeling ; Ultrafiltration
É parte de: Journal of chromatography, 1990, Vol.528 (2), p.357-369
Descrição: 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.
Editor: Netherlands: Elsevier B.V
Idioma: Inglês

Links

Voltar para lista de resultados