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. 1983 Apr;40(1):91–96. doi: 10.1128/iai.40.1.91-96.1983

Isolation and characterization of F12 adhesive fimbrial antigen from uropathogenic Escherichia coli strains.

P Klemm, I Orskov, F Orskov
PMCID: PMC264821  PMID: 6339412

Abstract

The adhesive fimbrial antigen F12 from a strain of uropathogenic Escherichia coli has been isolated and characterized. The antigen was purified by ammonium sulfate precipitation and gel chromatography. The protein subunit of the F12 fimbria has a molecular weight of 18,200; the N-terminal amino acid sequence of the subunit shows close resemblance to that of the subunits of other F fimbriae and the type 1 fimbriae. We identified in these proteins a pattern of alternating conserved and variable amino acid residues which could indicate a special structural and functional feature.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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