Autor: |
Riley, George R., West, Christopher M., Henderson, Ellen J. |
Zdroj: |
Glycobiology; Mar1993, Vol. 3 Issue 2, p165-177, 13p |
Abstrakt: |
The prestalk and prespore cells from the multicellular slug stage of development differ in assembly of glycoconjugates. Prespore cells are 2- to 3-fold more active than prestalk cells in the assembly of N-linked glycans and 20-fold more active in their fucosylation. Only prespore cells synthesize an O-linked glycan consisting in part of Fuc α-linked to -acetylglucosamine. Incorporation of fucose, glucosamine, mannose and galactose into large pronase-resistant glycoconjugates was almost exclusively into prespore cells. Such glucosamine-labelled glycoconjugates resist fragmentation by β-elimination and include a glycoantigen dependent on the B genetic locus. In contrast, large fucose-labelled glycoconjugates consisted of multiple, small, O-linked oligosaccharides on carrier peptides. The spore coat protein SP96 has several fucosylated O-linked oligosaccharides, one of which correlates with a fucose epitope previously shown to localize in prespore vesicles and the outer layer of the spore coat. [ABSTRACT FROM PUBLISHER] |
Databáze: |
Complementary Index |
Externí odkaz: |
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