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Eur J Biochem. 1995 Apr 1;229(1):308-15.

Characterization of the glycan structure of a major glycopeptide from the surface layer glycoprotein of Clostridium thermosaccharolyticum E207-71.

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Institute for Biological Sciences, National Research Council, Ottawa, Canada.


The squarely arranged surface layer (S-layer) glycoprotein of Clostridium thermosaccharolyticum E207-71 was isolated from bacterial cells which were grown under defined culture conditions. By sodium dodecyl sulfate polyacrylamide gel electrophoresis, the S-layer showed a series of distinct bands with apparent molecular masses in the range 83-210 kDa. Upon deglycosylation by trifluoromethanesulfonic acid, only the single band at 83 kDa remained unchanged. After pronase digestion of the intact S-layer glycoprotein, the degradation products were isolated by gel-permeation chromatography, cation-exchange chromatography and isoelectric focusing. Three main fractions and an amino sugar containing minor fraction were obtained. The main fractions, which showed identical carbohydrate compositions, were further purified by reverse-phase chromatography and characterized by monosaccharide analysis, Smith degradation, methylation analysis, and one-dimensional and two-dimensional nuclear magnetic resonance spectroscopy. The combined chemical and spectroscopical evidence suggest the following glycan structure for the main fractions: [Sequence: See text].

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