Involvement of dolicholmonophosphate in the formation of specific mannosyl-linkages in yeast glycoproteins

A membrane fraction from Saccharomyces cerevisiae catalyzes the transfer of mannosyl residues from GDP-Man partly via dolicholmonophosphate into a heterogenous glycoprotein fraction. The pattern of radioactive products obtained after mannosylation with GDP-[ 14C]Man is similar to that obtained with...

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Veröffentlicht in:Biochemical and biophysical research communications 1973-10, Vol.54 (3), p.1119-1124
Hauptverfasser: Babczinski, P., Tanner, W.
Format: Artikel
Sprache:eng
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Zusammenfassung:A membrane fraction from Saccharomyces cerevisiae catalyzes the transfer of mannosyl residues from GDP-Man partly via dolicholmonophosphate into a heterogenous glycoprotein fraction. The pattern of radioactive products obtained after mannosylation with GDP-[ 14C]Man is similar to that obtained with dolicholmonophosphate-[ 14C]mannose. In each case more than 70% of the radioactivity can be released by β-elimination. Evidence is presented, that only the mannosyl residue directly linked to protein is incorporated via dolicholmonophosphate.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(73)90808-5