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Journal Article

Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein

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Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., et al. (1992). Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein. Biological Chemistry Hoppe-Seyler., 373(4), 171-176.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-73F1-5
Abstract
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.