Chemical characterization of the regularly arranged surface layer glycoprotein of Clostridium thermosaccharolyticum D120-70.
Clostridium 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).
Altman
E
E
Division of Biological Sciences, National Research Council, Ottawa, Canada.
Brisson
J R
JR
Messner
P
P
Sleytr
U B
UB
D001426:Bacterial Proteins / Q000302:isolation & purification*; D002240:Carbohydrate Sequence; D003013:Clostridium / Q000032:analysis* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D008401:Gas Chromatography-Mass Spectrometry; D006020:Glycopeptides / Q000302:isolation & purification; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008562:Membrane Glycoproteins / Q000302:isolation & purification* / Q000648:ultrastructure; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000302:isolation & purification*; D011135:Polysaccharides, Bacterial / Q000032:analysis; D014312:Trisaccharides / Q000032:analysis
D001426:Bacterial Proteins; D006020:Glycopeptides; D008562:Membrane Glycoproteins; D011134:Polysaccharides; D011135:Polysaccharides, Bacterial; D014312:Trisaccharides