title: [Purification and some properties of "Clostridium perfringens" delta toxin (author's transl)].
abstract: Delta toxin, a hemolytic exocellular protein excreted by C. perfringens type C has been purified to homogeneity, assessed by polyacrylamide disc gel electrophoresis. Purification steps involved successively calcium phosphate gel formation in culture supernatant fluid, salting-out of unadsorbed material by ammonium sulfate to 50 % saturation, isoelectric focusing and gel filtration on Sephadex G75. Purified toxin appears as a basic protein occuring in two forms with isoelectric points of 8.8 and 9.4 as disclosed by isoelectric focusing. Molecular weight estimated by SDS-polyacrylamide disc gel electrophoresis was found to be close to 42,000 for the two forms. The lytic activity of delta toxin is inhibited by Ca++ and EDTA. The toxin is activated by short-term treatment with low concentration of trypsin.
mesh_terms: D000645:Ammonium Sulfate; D002130:Calcium Phosphates; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003016:Clostridium perfringens; D004591:Electrophoresis, Polyacrylamide Gel; D006461:Hemolysis; D007525:Isoelectric Focusing; D008970:Molecular Weight; D014118:Toxins, Biological / Q000032:analysis / Q000302:isolation & purification*; D014357:Trypsin / Q000494:pharmacology
chemical_list: D002130:Calcium Phosphates; D014118:Toxins, Biological; D014357:Trypsin; D000645:Ammonium Sulfate
vernacular_title: Essai de purification et propriétés de la toxine delta de Clostridium perfringens type C