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Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis.

The gene coding for the sialic acid-specific adhesin SfaS produced by the S fimbrial adhesin (sfa) determinant of Escherichia coli has been modified by oligonucleotide-directed, site-specific mutagenesis. Lysine 116, arginine 118, and lysine 122 were replaced by threonine, serine, and threonine, res...

詳細記述

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書誌詳細
出版年:Infect Immun
主要な著者: Morschhäuser, J, Hoschützky, H, Jann, K, Hacker, J
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Microbiology (ASM) 1990
主題:
オンライン・アクセス:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC258787/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2194961/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.58.7.2133-2138.1990
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