ausblenden:
Schlagwörter:
Amino Acid Sequence; *Bacteria, Anaerobic/ch [Chemistry]; *Bacterial Outer Membrane Proteins/ch [Chemistry]; *Glycosaminoglycans/ch [Chemistry]; Molecular Sequence Data; Peptides/ch [Chemistry]; *Tyrosine/ch [Chemistry]
Zusammenfassung:
The S-layer protein of Acetogenium kivui was subjected to proteolysis with different proteases and several high molecular mass glycosaminoglycan peptides containing glucose, galactosamine and an unidentified sugar-related component were separated by molecular sieve chromatography and reversed-phase HPLC and subjected to N-terminal sequence analysis. By methylation analysis glucose was found to be uniformly 1,6-linked, whereas galactosamine was exclusively 1,4-linked. Hydrazinolysis and subsequent amino-acid analysis as well as two-dimensional NMR spectroscopy were used to demonstrate that in these peptides carbohydrate was covalently linked to tyrosine. As all of the four Tyr-glycosylation sites were found to be preceded by valine, a new recognition sequence for glycosylation is suggested.
