title: Structure of the glycan chain from the surface layer glycoprotein of Bacillus alvei CCM 2051.
abstract: The 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.
authors.affiliation: Institute for Biological Sciences, National Research Council, Ottawa, Ont., Canada.
authors.forename: E
authors.initials: E
authors.lastname: Altman
authors.forename: J R
authors.initials: JR
authors.lastname: Brisson
authors.forename: P
authors.initials: P
authors.lastname: Messner
authors.forename: U B
authors.initials: UB
authors.lastname: Sleytr
mesh_terms: D001407:Bacillus / Q000032:analysis* / Q000648:ultrastructure; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005613:Freeze Etching; D006023:Glycoproteins / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D008745:Methylation; D015394:Molecular Structure; D008970:Molecular Weight; D011134:Polysaccharides / Q000737:chemistry*
chemical_list: D006023:Glycoproteins; D011134:Polysaccharides