Glycosylation of ribonuclease A catalysed by rabbit liver extracts

Z. Khalkhali, R. D. Marshall

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Crude extracts of rabbit liver catalyse in vitro the transfer of N acetylglucosamine from uridine diphosphate N acetylglucosamine to bovine pancreatic ribonuclease A. The enzymic activity is contained in rough endoplasmic reticulum. It has an absolute requirement for a bivalent metal ion: Co2+>Mn2+>Ni2+ Mg2+ is ineffective. There is enzymic activity in the absence of detergent, but increased activity is observed in the presence of Triton X 100. The site of glycosylation of ribonuclease A is asparagine 34, and glycosylation occurs only at this point. These findings agree with the hypothesis that the sequence Asn X Thr(Ser) (where X may be one of a number of types of amino acid) is a necessary, but not sufficient, condition for N acetylglucosaminylation of a protein bound asparagine residue.

Original languageEnglish (US)
Pages (from-to)299-307
Number of pages9
JournalBiochemical Journal
Issue number2
StatePublished - Dec 1 1975

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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