UDP-N-Acetyl-D-glucosamine-Asparagine sequon N-Acetyl-β-D-Glucosaminyl -Transferase-Activity in Human serum

Zhila Khalkhali*, R. Derek Marshall

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Serum contains a sugar transferase which is able to catalyse the glycosylation in in vitro of the asparagine residue present in the sequence Asn.Leu.Thr in bovine pancreatic ribonuclease. UDP-2-Acetamido-2-deoxy-D-glucose (UDP-N-acetyl-D- glucosamine) acts as the donor, although the mechanism of the transfer is unexplored. Spermidine and Mn2+, as well as CDP-choline, can act as activators for the reaction. Monoglycosylated ribonuclease (ribonuclease-GIcNAc) has been separated (23% yield) from unreacted ribonuclease A by affinity chromatography on a colunm of wheat-germ agglutinin bound to Sepharose, and characterised. A possible reason for the presence of the enzyme in serum is suggested.

Original languageEnglish (US)
Pages (from-to)455-473
Number of pages19
JournalCarbohydrate Research
Issue numberC
StatePublished - Jul 1976

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry


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