[Purification and characterization of "Clostridium perfringens" BP6K-N5 strain bacteriocin N5 (author's transl)].
The bacteriocin N5 produced by Clostridium perfringens, strain BP6K-N5, after UV irradiation induction, was purified by ammonium sulfate precipitation, followed by ion-exchange chromatography on DEAE cellulose and gel filtration on Sephadex G100. By polyacrylamid-gel electrophoresis and immunodiffusion analysis the purified material was shown to be homogenous. The purified bacteriocin N5 is inactivated by proteolytic enzymes and by heat treatment at 50 degrees C for 15 minutes. It is a simple protein with a molecular weight of approximately 82.000. The protein appears to be a single polypeptide chain, as no dissociation is obtained by sodium dodecyl sulfate and beta-mercaptoethanol disc-gel-electrophoresis.
D001430:Bacteriocins / Q000276:immunology / Q000302:isolation & purification*; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003016:Clostridium perfringens / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008970:Molecular Weight; D011487:Protein Conformation
D001430:Bacteriocins
Purification et caractérisation de la bactériocine N5 de Clostridium perfringens BP6K-N5 TYPE A