Abstract
The outer membrane of Pseudomonas aeruginosa PA01 is permeable to saccharides of molecular weights lower than about 6000. Triton X-100/EDTA-soluble outer membrane proteins were fractionated by ion-exchange chromatography in the presence of Triton X-100 and EDTA, and the protein contents of the various fractions analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Each of the major protein bands present in the Triton X-100/EDTA soluble outer membrane was separated from one another. Adjacent fractions were pooled, concentrated and extensively dialyzed to reduce the Triton X-100 concentration. Vesicles were reconstituted from lipopolysaccharide, phospholipids and each of these dialyzed fractions, and examined for their ability to retain [14C]sucrose. Control experiments indicated that the residual levels of Triton X-100 remaining in the dialyzed fractions had no effect on the formation or permeability to saccharides of the reconstituted vesicles. It was concluded that a major outer membrane polypeptide with an apparent weight of 35 000 is a porin, responsible for the size-dependent permeability of the outer membrane.
Original language | English |
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Pages (from-to) | 323-331 |
Number of pages | 9 |
Journal | BBA - Biomembranes |
Volume | 554 |
Issue number | 2 |
DOIs | |
Publication status | Published or Issued - 5 Jul 1979 |
Externally published | Yes |
Keywords
- (Pseudomonas aeruginosa, Outer membrane)
- Membrane protein
- Permeability
- Porin
- Reconstitution
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology