| | 1 | Author
| Stefan Stevanovic, Günther Jung, JürgP. Rosenbusch | Requires cookie* | | | Title
|  | | | | Abstract
| The major outer membrane protein of Rhodobacter capsulatus 37b4 (capsule-free) was iso lated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer mem branes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band (M T above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro phoresis and dissociated into a single species of polypeptides (M r 36,000) on treatment with EDTA (10 m M at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed G lu-V al-Lys-Leu-Ser-G ly-A sp-Ala-Arg-M et-G ly-V al-M et-T yr-A sn-Gly-A sp-Asp-X-A sn-Phe-Ser-Ser. | | | |
Reference
| Z. Naturforsch. 45c, 576—582 (1990); received February 19 1990 | | | |
Published
| 1990 | | | |
Keywords
| Rhodobacter capsulatus, Cell Wall, Outer Membrane, Porin, Oligomeric Structure | | | |
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| default:Reihe_C/45/ZNC-1990-45c-0576.pdf | | | | Identifier
| ZNC-1990-45c-0576 | | | | Volume
| 45 | |
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