|
|||||
|
|
Afimbrial adhesin from Escherichia coli strain 2230: Purification, characterization and partial covalent structure |
|
| Authors: | Christiane Forestier Karen G. Welinder Arlette Darfeuille-Michaud Per Klemm |
| Affiliation: | Services de Bactériologie-Virologie, Universitéde Clermont I, Clermont-Ferrand, France;Institute of Biochemical Genetics, University of Copenhagen, Copenhagen, Denmark;Department of Microbiology, Technical University of Denmark, Lyngby, Denmark |
| Abstract: | The afimbrial adhesive factor from human enterotoxigenic Escherichia coli strain 2230 was isolated. The adhesin was removed from the cells by heat treatment. The purification procedure included ammonium sulfate precipitation and column chromatography on Sepharose CL-6B in the presence of guanidine hydrochloride. The purified adhesin was a 16-kDa protein with an isoelectric point of 4.4. The amino acid sequence of the N-terminal 29 amino acid residues showed significant homology with that of several fimbrial proteins of E. coli. |
| Keywords: | Escherichia coli Adhesion Adhesion Outer membrane protein (Afrimbrial adhesin) |
| 本文献已被 ScienceDirect 等数据库收录！ | |