Structure of the glycan chain from the surface layer glycoprotein of Clostridium thermohydrosulfuricum L77-66: Biochim.Biophys Acta

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TypeArticle
Journal titleBiochim.Biophys Acta
Volume1117
Issue1
Pages7177; # of pages: 7
SubjectACID; analysis; bacterial; Bacterial Outer Membrane Proteins; BAND; Canada; carbohydrate; Carbohydrate Sequence; cell; Cell Wall; CHAIN; chemical; chemistry; Chromatography,Gel; Clostridium; complex; COMPLEXES; deglycosylation; Digestion; Electrophoresis; Filtration; Freeze Etching; GLYCAN CHAIN; glycopeptide; glycoprotein; Glycoproteins; HETERONUCLEAR; homonuclear; isolation & purification; MAGNETIC; Magnetic Resonance Spectroscopy; MAGNETIC-RESONANCE; Mass Fragmentography; membrane; Membrane Glycoproteins; Membrane Proteins; Mesylates; Methylation; Models,Molecular; MOLECULAR; Molecular Sequence Data; NUCLEAR; Nuclear Magnetic Resonance; NUCLEAR-MAGNETIC-RESONANCE; POLYSACCHARIDE; Polysaccharides; protein; Proteins; RESONANCE; Sodium; structure; SUBUNIT; Support,Non-U.S.Gov't; surface; ultrastructure
AbstractThe thermophilic eubacterium Clostridium thermohydrosulfuricum L77-66 is covered by a crystalline surface layer composed of identical glycoprotein subunits which are arranged in a hexagonal lattice with centre-to-centre spacings of approx. 14.3 nm. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of cell wall preparations showed the presence of several broadened, carbohydrate-containing bands in a molecular mass range of 90 to 200 kDa. A total carbohydrate content of approx. 14% was determined in the purified surface layer glycoprotein. Chemical deglycosylation of this material by trifluoromethanesulfonic acid resulted in the disappearance of the complex banding pattern. Only a single band with a molecular mass of 82 kDa remained visible upon Coomassie staining. After proteolytic digestion of the surface layer glycoprotein a single glycopeptide fraction with an apparent molecular mass of approx. 25 kDa was obtained by gel filtration. Composition analysis, methylation, periodate oxidation and a combination of homonuclear and 1H-detected heteronuclear shift-correlated nuclear magnetic resonance experiments established the following structure for the glycan chain of the surface layer glycoprotein
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberALTMAN1992
NPARC number9367195
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Record identifier515149bf-17c0-450b-833e-117d89b7d122
Record created2009-07-10
Record modified2016-05-09
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