Channel-Forming (Porin) Activity in Herpetosiphon aurantiacus Hp a2
AUTOR(ES)
Harwardt, Rainer
FONTE
American Society for Microbiology
RESUMO
Detergent extracts of cell envelopes of the gliding bacterium Herpetosiphon aurantiacus formed channels in lipid bilayers. Fast protein liquid chromatography across a HiTrap-Q cation-exchange column demonstrated that a 45-kDa protein forms the channel. The observation of a channel-forming protein suggests that Herpetosiphon aurantiacus Hp a2 has a permeability barrier on its surface.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=516602Documentos Relacionados
- Secondary structure of a channel-forming protein: porin from E. coli outer membranes.
- Identification of channel-forming activity in the cell wall of Corynebacterium glutamicum.
- Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers.
- Induction of epithelial chloride secretion by channel-forming cryptdins 2 and 3
- All-D amino acid-containing channel-forming antibiotic peptides.