The capsular (K51) antigen of Escherichia coli 01:K51:H−, an O-acetylated poly-N-acetylglucosamine phosphate |
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Authors: | Barbara Jann Thomas Dengler Klaus Jann |
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Affiliation: | Max-Planck-Institut für Immunbiologie, D7800 Freiburg, F.R.G. |
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Abstract: | Abstract The capsular K51 antigen of E.coli was isolated from a liquid culture of E.coli 01:K51:H− by Cetavlon precipitation. After purification it was obtained in a yield of about 80 mg/l. The polymer consisted of equimolar amounts of N -acetylglucosamine and phosphate and contained about 1.6 O -acetyl groups per N -acetylglucosamine residue. After de- O -acetylation it was resistant to periodate oxidation. Mild acid hydrolysis yielded N -acetylglucosamine-3-phosphate. With the aid of 13C- and 31P-NMR spectroscopy it was ascertained that the K51 antigen is a poly- α -1.3- N -acetylglucosamine phosphate, in which most of the hydroxyl groups at C4 and C6 of the N -acetylglucosamine residue are acetylated. |
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