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Purification and partial characterization of an iron regulated outer membrane protein of B. fragilis under
B R Otto1, A M Verweij-Van Vught, D M Maclaren
1Department of Medical Microbiology, Medical School Vrije Universiteit, Amsterdam, The Netherlands.
FEMS Microbiology Letters
|January 1, 1990
Abstract:
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.