Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194560
Type: Artigo de periódico
Title: Purification And Characterization Of The Fimbria F18ac (2134p) Isolated From Enterotoxigenic Escherichia Coli (etec).
Author: Amorim, C R
Matsuura, M S
Rosa, J C
Greene, L J
Leite, D S
Yano, T
Abstract: The adhesin F18ac purified on Sepharose CL 4B column chromatography and SDS-PAGE stained with Coomassie Blue and Western blotting using specific anti-F18ac serum presented one band of approximately 17kDa. Gold immunolabeling revealed that the adhesin F18ac has a fimbrial structure on the bacterial surface. The first 27 amino acid residues of the N-terminal portion of the adhesin F18ac, showed 92.5% homology (25 amino acids) with the F107 (F18ab) fimbriae.
Subject: Adhesins, Escherichia Coli
Amino Acid Sequence
Animals
Blotting, Western
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Escherichia Coli
Fimbriae, Bacterial
Molecular Sequence Data
Swine
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/10925040
Date Issue: 2000
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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