Theta-toxin of Clostridium perfringens. I. Purification and some properties.
Theta-Toxin, an oxygen-labile hemolysin produced by Clostridium perfringens, was purified 3300 fold from culture filtrate by successive chromatography on DEAE-Sephadex A-50 and Sephadex G-150. The purified toxin gave two distinct bands in disc electrophoresis, while the same material, after mild reduction with dithiothreitol, yielded a single band, indicating that the purified theta-toxin contained, as well as a reduced, active form, an oxidized, inactive form of toxin. These two forms of the toxin had a similar, if not identical molecular size. The purified preparation gave a single band in a sodium dodecyl sulfate polyacrylamide gel electrophoresis and formed a single precipitin line with National Standard gas gangrene (C. perfringens) antitoxin. By sodium dodecyl sulfate polyacrylamide gel electrophoresis, the molecular weight of theta-toxin was estimated to be 51 000, the value being in exact accordance with that obtained by amino acid analysis. The amino acid composition of theta-toxin was very close to that of cereolysin, an oxygen-labile hemolysin produced by Bacillus cereus. The amino-terminal residue of theta-toxin was lysine as determined by the Dansyl method.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001427:Bacterial Toxins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003016:Clostridium perfringens; D004591:Electrophoresis, Polyacrylamide Gel; D006460:Hemolysin Proteins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship
D000596:Amino Acids; D001427:Bacterial Toxins; D006460:Hemolysin Proteins