Purification and partial characterization of an iron regulated outer membrane protein of B. fragilis under non-denaturing conditions | Zendy

B Otto | Zendy

Open Access

Purification and partial characterization of an iron regulated outer membrane protein of B. fragilis under non-denaturing conditions

Author(s) -

B Otto

Publication year - 1990

Publication title -

fems microbiology letters

Language(s) - English

Resource type - Journals

eISSN - 1574-6968

pISSN - 0378-1097

DOI - 10.1016/0378-1097(90)90298-5

Subject(s) - bacteroides fragilis , chaps , bacterial outer membrane , isoelectric point , membrane protein , membrane , chemistry , isoelectric focusing , biochemistry , protein purification , biology , chromatography , escherichia coli , gene , enzyme , antibiotics

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.

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