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 |
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Hauptverfasser: | , |
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. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(73)90808-5 |