| Literature DB >> 7340813 |
W H Ward, P Britton, S van Heyningen.
Abstract
1. Charge-shift electrophoresis showed that cholera toxin and its subunits have no hydrophobic surfaces. 2. Amino-acid composition and sequence data suggested that the proteins have no masked hydrophobic regions. 3. The A subunit of cholera toxin may interact with polar molecules in the membrane to exert its effect inside the cell. 4. The only hydrophobic part of tetanus toxin was the H-chain.Entities:
Mesh:
Substances:
Year: 1981 PMID: 7340813 PMCID: PMC1163391 DOI: 10.1042/bj1990457
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857