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.
Original language | English (US) |
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Pages (from-to) | 83-86 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 275 |
Issue number | 1-2 |
DOIs | |
State | Published - Nov 26 1990 |
Externally published | Yes |
Keywords
- GM1
- Ganglioside
- Glycolipid
- Glycosyltransferase
- Sialyltransferase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology