Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola.
AUTOR(ES)
Egli, C
RESUMO
A 53-kDa protein from the outer sheath of the oral spirochete Treponema denticola was purified to homogeneity and shown to reconstitute channels in black lipid bilayer model membranes. The channel had a single-channel conductance of 1.8 nS in 0.1 M KCl, making this the largest porin channel observed to date (estimated diameter, 3.4 nm). Electron micrographs of 53-kDa-protein-containing outer sheaths of T. denticola showed a regular hexagonal array of darker staining pits.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=280753Documentos Relacionados
- Characterization, cloning, and binding properties of the major 53-kilodalton Treponema denticola surface antigen.
- Pore-forming ability of major outer membrane proteins from Wolinella recta ATCC 33238.
- Biochemical properties of the outer membrane of Treponema denticola.
- Carbohydrate-reactive, pore-forming outer membrane proteins of Aeromonas hydrophila.
- A major antigen on the outer envelope of a human oral spirochete, Treponema denticola.