Article
Clostridium septicum alpha-toxin is proteolytically activated by furin.
Infection and immunity - 1 Oct 1997
Gordon V M, Benz R, Fujii K, Leppla S H, Tweten R K
Abstract excerpt
Clostridium septicum alpha-toxin is secreted as an inactive 46,450-Da protoxin. The protoxin is activated by proteolytic cleavage near the C terminus, which eventually causes the release of a 45-amino-acid fragment. Proteoytic activation and loss of the propeptide allow alpha-toxin to oligomerize...
Topics
- Animals
- Antipain
- Bacterial Toxins
- CHO Cells
- Clostridium
- Cricetinae
- Cysteine Proteinase Inhibitors
- Dose-Response Relationship, Drug
- Furin
- Hemolysis
- Mutation
- Propidium
- Protein Processing, Post-Translational
- Recombinant Proteins
- Subtilisins
- Toxicity Tests
- Trypsin
