SDS-soluble and peptidoglycan-bound proteins in the outer membrane-peptidoglycan complex of Brucella abortus | Academic Article individual record
abstract

Outer membrane-peptidoglycan complex from Brucella abortus was separated from cytoplasmic membrane and cytosol by either sucrose density gradient fractionation or differential (rate) centrifugation of surface labeled cells disrupted by sonication without the use of detergents. The outer membrane-peptidoglycan complex had a buoyant density of 1.22 gm/ml and contained 67 labeled SDS-soluble proteins when examined by SDS-PAGE. Included were four major bands exhibiting molecular masses of 88k, 40k, 35.7k and 26k daltons corresponding to previously described group 1, 2 and 3 outer membrane proteins. Lysozyme treatment of outer membrane-peptidoglycan complex increased its buoyant density to 1.25 gm/ml and released eight additional peptidoglycan-linked proteins.

author list (cited authors)
Sowa, B. A., Kelly, K. A., Ficht, T. A., Frey, M., & Adams, L. G.
publication date
1991
publisher
Elsevier bv Publisher
published in
keywords
  • Autoradiography
  • Bacterial Outer Membrane Proteins
  • Animals
  • Sodium Dodecyl Sulfate
  • Microscopy, Electron
  • Peptidoglycan
  • Immunoblotting
  • Electrophoresis, Polyacrylamide Gel
  • Centrifugation, Density Gradient
  • Solubility
  • Brucella Abortus
altmetric score

6.0

citation count

31