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

From National Research Council Canada

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FormatText, Article
Subjectacid; amino acid sequence; bacterial; band; Canada; carbohydrate sequence; cell; chemical; chemistry; chromatography; clostridium; deglycosylation; degradation; digestion; electrophoresis; glycopeptide; glycoprotein; isoelectric focusing; magnetic; magnetic resonance spectroscopy; membrane; membrane glycoproteins; methylation; methylation analysis; molecular; molecular sequence data; molecular structure; nuclear; nuclear magnetic resonance; nuclear magnetic resonance spectroscopy; one-dimensional; polysaccharide; polysaccharides; Pronase; resonance; series; sodium; sodium dodecyl sulfate; spectroscopy; structure; sugar; sulfate; Support, Non-U. S. Gov't; surface
Abstract
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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In
  • European Journal of Biochemistry 229, no. 1 (1 April 1995): 308–315.
LanguageEnglish
Peer reviewedYes
NRC numberALTMAN1995
NPARC number9359359
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Record created2009-07-10
Record modified2020-04-29
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