Article
Elimination of the disulphide bridge in fragment B of diphtheria toxin: effect on membrane insertion, channel formation, and ATP binding.
Molecular microbiology - 1 Mar 1991
Stenmark H, Olsnes S, Madshus I H
Abstract excerpt
Active diphtheria toxin consists of two disulphide-linked fragments, termed A and B. Fragment B, which contains an internal disulphide bridge, facilitates translocation of the enzymatically active fragment A to the cytosol of eukaryotic cells. In this process cation-selective channels are formed....
Topics
- Adenosine Triphosphate
- Animals
- Cell Membrane
- Cell Membrane Permeability
- Corynebacterium diphtheriae
- Diphtheria Toxin
- Disulfides
- Mutation
- Peptide Fragments
- Sodium
- Sodium Channels
- Trypsin
- Vero Cells