Purification to homogeneity of GD3 synthase and partial purification of GM3 synthase from rat brain

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

Research output: Contribution to journalArticle

23 Scopus citations


A CMP-sialic acid: GM3 sialyltransferase (GD3 synthase) and a CMP-sialic acid: LacCer sialyltransferas (GM3 synthase) have been purified 10,000- and 3,000-fold, respectively, from the Triton X-100 extract of rat brain. The two enzymes were purified and resolved by affinity chromatography on two successive CDP-Sepharose columns by NaCl gradient elution. Final purification of GD3 synthase was achieved by specific elution from a 'GM3 acid'-Sepharose column with buffer containing GM3. Sodium dodecylsulfate-gel electrophoresis of GD3 synthase revealed a single major protein band with an apparent molecular weight of 55,000.

Original languageEnglish (US)
Pages (from-to)387-393
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Jan 15 1990
Externally publishedYes


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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