[Purification of an extracellular thiol-dependent hemolysin from Bacillus alvei].
Alveolysin a sulfhydryl-dependent cytolytic extracellular protein released by Bacillus alvei has been purified by salting-out by ammonium sulfate, gel filtration, isoelectric focusing on pH gradient and chromatography on DEAE-cellulose. The purified protein after reduction by thiols (active hemolytic form) proved homogeneous by disc polyacrylamide gel electrophoresis and by gel immunodiffusion. The molecular weight was 60,000 daltons, Two molecular forms of pI 5.1 and 7.0 were detected by gel isoelectrofocusing. The toxin was lethal to the mouse. Lytic activity was inhibited by cholesterol and antistreptolysin O anstisera. Immunological cross-reaction was observed between alveolysin and streptolysin O.
D001407:Bacillus / Q000032:analysis*; D003429:Cross Reactions; D006460:Hemolysin Proteins / Q000302:isolation & purification*; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D008970:Molecular Weight; D013439:Sulfhydryl Reagents
D006460:Hemolysin Proteins; D013439:Sulfhydryl Reagents; C014963:alveolysin
Purification de l'hémolysine thiol-dépendante extracellulaire de Bacillus alvei.