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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(corresponding author)
*Corresponding author for this work
  • Virginia Commonwealth University
Scholary Output:
Contribution to journal
Article
 Peer-review

Open access

Abstract

A CMP-NeuAc:GM1 α2-3sialyltransferase (GD1a synthase, 2.4.99.2) 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.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
 Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 83-86 (4 pages)

Journal (Volume, Issue Number)

FEBS Letters (Volume 275, Issue 1-2)

Publication milestones

  • Published - 11/26/1990

Publication status

Published - 11/26/1990

ISSN

0014-5793

Publication IDs

  • Scopus: 0025153401
  • PubMed: 2262006

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Funding Details

FunderFunding number
NINDS
R01NS011853