Chemical characterization of the regularly arranged surface layer glycoprotein of Clostridium thermosaccharolyticum D120-70

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TypeArticle
Journal titleEuropean Journal of Biochemistry
Volume188
Issue1
Pages7382; # of pages: 10
Subjectanalysis; Bacterial Proteins; BAND; Canada; Carbohydrate Sequence; cell; chemical; Clostridium; DEGRADATION; Electrophoresis,Polyacrylamide Gel; ENVELOPE; Glycopeptides; Glycoproteins; isolation & purification; MAGNETIC; Magnetic Resonance Spectroscopy; MAGNETIC-RESONANCE; Mass Fragmentography; Membrane Glycoproteins; Methylation analysis; Microscopy,Electron; Molecular Sequence Data; MOLECULE; Nuclear Magnetic Resonance; Polysaccharides,Bacterial; Proteins; RESONANCE; SPECTROSCOPIC; structure; Support,Non-U.S.Gov't; surface; Trisaccharides; ultrastructure
AbstractClostridium thermosaccharolyticum D120-70 possesses as its outermost cell envelope layer a square-arranged array of glycoprotein molecules. SDS/polyacrylamide gel electrophoresis of the purified surface layer showed a broadened band in the molecular mass range of about 115 kDa which, upon periodic acid/Schiff staining, gave a positive reaction. After proteolytic degradation of this material, two glycopeptide fractions were obtained. One- and two-dimensional nuclear magnetic resonance studies, together with methylation analysis and periodate oxidation, were used to determine the structures of the polysaccharide portions of these glycopeptides. The combined chemical and spectroscopic evidence suggests the following structures: (formula; see text)
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NRC numberALTMAN1990B
NPARC number9365415
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Record identifierb9772f55-20df-4a0c-99ae-854eeac7a8d0
Record created2009-07-10
Record modified2016-06-01
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