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

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TypeArticle
Journal titleEuropean Journal of Biochemistry
Volume229
Issue1
Pages308315; # of pages: 8
SubjectACID; Amino Acid Sequence; analysis; bacterial; BAND; Canada; Carbohydrate Sequence; CELLS; chemical; chemistry; Chromatography; Clostridium; deglycosylation; DEGRADATION; Digestion; Electrophoresis; glycopeptide; glycoprotein; Glycoproteins; Isoelectric Focusing; MAGNETIC; Magnetic Resonance Spectroscopy; MAGNETIC-RESONANCE; membrane; Membrane Glycoproteins; Methylation; Methylation analysis; MOLECULAR; Molecular Sequence Data; Molecular Structure; NUCLEAR; Nuclear Magnetic Resonance; nuclear magnetic resonance spectroscopy; NUCLEAR-MAGNETIC-RESONANCE; one-dimensional; POLYSACCHARIDE; Polysaccharides; Pronase; RESONANCE; SERIES; Sodium; Sodium Dodecyl Sulfate; SPECTROSCOPY; structure; sugar; SULFATE; Support,Non-U.S.Gov't; surface
AbstractThe 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]
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NRC numberALTMAN1995
NPARC number9359359
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Record identifier0a60ff60-7f89-4fff-94b0-7968db3f8611
Record created2009-07-10
Record modified2016-06-01
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