STRUCTURE OF THE GLYCAN CHAIN FROM THE SURFACE-LAYER GLYCOPROTEIN OF BACILLUS-ALVEI CCM-2051

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 [GRAPHICS] as the repeating unit for this glycan chain.