| Author | Search for: Altman, Eleonora; Search for: Brisson, J.; Search for: Messner, P.; Search for: Sleytr, U. |
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| Format | Text, Article |
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| Subject | 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 |
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| Abstract | 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) |
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| Publication date | 1990-02-22 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | ALTMAN1990B |
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| NPARC number | 9365415 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | b9772f55-20df-4a0c-99ae-854eeac7a8d0 |
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| Record created | 2009-07-10 |
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| Record modified | 2020-03-17 |
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