Purification and partial characterization of an iron regulated outer membrane protein of B. fragilis under non-denaturing conditions.
The CHAPS-PAGE gelsystem we applied gave a good separation of the proteins of Bacteroides fragilis under non-denaturing conditions. We succeeded with preparative CHAPS-PAGE in purifying an iron regulated outer membrane protein (a 44 kDa polypeptide on SDS-PAGE) of B. fragilis. This integral membrane protein proved to be a lipopolysaccharide binding protein with an isoelectric point of approximately pH 5.5. This method of purifying membrane proteins could be an important step in research into the function of membrane proteins.
Otto
B R
BR
Department of Medical Microbiology, Medical School Vrije Universiteit, Amsterdam, The Netherlands.
Verweij-Van Vught
A M
AM
Maclaren
D M
DM
D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D001441:Bacteroides fragilis / Q000378:metabolism*; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism; D002793:Cholic Acids; D004591:Electrophoresis, Polyacrylamide Gel; D007501:Iron / Q000378:metabolism*; D007526:Isoelectric Point; D008070:Lipopolysaccharides / Q000378:metabolism; D008970:Molecular Weight; D011489:Protein Denaturation
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D002793:Cholic Acids; D008070:Lipopolysaccharides; D007501:Iron; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate