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

24 Citations (Scopus)

Abstract

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
Volume166
Issue number1
DOIs
StatePublished - Jan 15 1990
Externally publishedYes

Fingerprint

Cytidine Monophosphate N-Acetylneuraminic Acid
Sepharose
Purification
Rats
Brain
Cytidine Diphosphate
Sialyltransferases
Affinity chromatography
Distillation columns
Octoxynol
Electrophoresis
Affinity Chromatography
Buffers
Molecular Weight
Gels
Sodium
Molecular weight
Acids
Enzymes
Proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Purification to homogeneity of GD3 synthase and partial purification of GM3 synthase from rat brain. / Gu, Xin Bin; Gu, Tian Jue; Yu, Robert K.

In: Biochemical and Biophysical Research Communications, Vol. 166, No. 1, 15.01.1990, p. 387-393.

Research output: Contribution to journalArticle

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