SDS-soluble and peptidoglycan-bound proteins in the outer membrane-peptidoglycan complex of Brucella abortus. Academic Article

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.

authors

• Adams, Leslie
• Ficht, Thomas

published proceedings

• Vet Microbiol

altmetric score

• 6

author list (cited authors)

• Sowa, B. A., Kelly, K. A., Ficht, T. A., Frey, M., & Adams, L. G.

citation count

• 32

complete list of authors

• Sowa, BA||Kelly, KA||Ficht, TA||Frey, M||Adams, LG

publication date

• January 1991

publisher

• Elsevier  Publisher

published in

• Veterinary Microbiology  Journal

keywords

• Animals
• Autoradiography
• Bacterial Outer Membrane Proteins
• Brucella Abortus
• Centrifugation, Density Gradient
• Electrophoresis, Polyacrylamide Gel
• Immunoblotting
• Microscopy, Electron
• Peptidoglycan
• Sodium Dodecyl Sulfate
• Solubility

PubMed Central ID

• 1909068

Digital Object Identifier (DOI)

• 10.1016/0378-1135(91)90160-h

start page

• 351

end page

• 369

volume

• 27

issue

• 3-4

URL

• http://dx.doi.org/10.1016/0378-1135(91)90160-h