Structure of the glycan chain from the surface layer glycoprotein of Bacillus alvei CCM 2051: Biochem.Cell Biol.

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TypeArticle
Journal titleBiochem.Cell Biol.
Volume69
Issue1
Pages7278; # of pages: 7
Subjectanalysis; Bacillus; BAND; Canada; Carbohydrate Conformation; Carbohydrate Sequence; cell; CELL-SURFACE; CHAIN; chemistry; DEGRADATION; Electrophoresis; Electrophoresis,Polyacrylamide Gel; Freeze Etching; GLYCAN CHAIN; glycopeptide; glycoprotein; Glycoproteins; MAGNETIC; Magnetic Resonance Spectroscopy; MAGNETIC-RESONANCE; Methylation; Methylation analysis; MOLECULAR; Molecular Structure; Molecular Weight; NUCLEAR; Nuclear Magnetic Resonance; NUCLEAR-MAGNETIC-RESONANCE; POLYSACCHARIDE; Polysaccharides; REPEATING UNIT; RESONANCE; Sodium; Sodium Dodecyl Sulfate; structure; SUBUNIT; SULFATE; Support,Non-U.S.Gov't; surface; TRISACCHARIDE; ultrastructure; UNIT
AbstractThe cell surface of the mesophilic eubacterium Bacillus alvei CCM 2051 is covered by an oblique arranged surface layer glycoprotein. The subunits revealed by sodium dodecyl sulfate - polyacrylamide gel electrophoresis were distinct bands of molecular masses 140,000, 128,000, and 127,000. Proteolytic degradation of the purified S-layer glycoprotein yielded a single glycopeptide fraction with an apparent molecular mass of ca. 25,000. Methylation analysis in conjunction with two-dimensional nuclear magnetic resonance experiments at 500 MHz established the branched trisaccharide (formula; see text) as the repeating unit for this glycan chain
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberALTMAN1991A
NPARC number9360703
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Record identifier492586f3-8239-4888-8931-1dad798ddbb7
Record created2009-07-10
Record modified2016-05-09
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