Purification and characterization of CMP-NeuAc:GM1 (Galβ1-4Ga1NAc) α2-3 sialyltransferase from rat brain

Tian Jue Gu, Xin Bin Gu, Toshio Ariga, Robert K. Yu

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


A CMP-NeuAc:GM1 α2-3sialyltransferase (GD1a synthase, has been purified from the Triton extract of rat brain. The enzyme was purified and resolved by affinity chromatography on CDP-Sepharose column by a linear NaCl gradient elution. Final purification was achieved by elution from a 'GM1-acid'-Sepharose column. SDS-PAGE of the enzyme revealed a single protein band with an apparent Mr 44 kDa. It catalyzed specifically the sialylation of GD1b, GM1 and asialo-GM1. Enzyme products were identified by TLC in three different solvent systems, The Km value for GM1 was 7.5 × 10-2 M, and for CMP-NeuAc it was 6.5 × 10-5 M.

Original languageEnglish (US)
Pages (from-to)83-86
Number of pages4
JournalFEBS Letters
Issue number1-2
StatePublished - Nov 26 1990
Externally publishedYes


  • GM1
  • Ganglioside
  • Glycolipid
  • Glycosyltransferase
  • Sialyltransferase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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