Abstract
A high resolution capillary electrophoresis method is developed for monitoring enzymatic reactions catalyzed by glycosyltransferases. Under inverted electroosmotic flow conditions at pH 2.5, the method quantifies UDP, UDP-Gal, UDP-Glc, and UDP-GlcNAc in the range of 10 to 150 μM. Enzyme activity of α-1,3-galactosyltransferase was determined by monitoring the formation of UDP subproduct formed in the transglycosylation reaction. The method is fast and versatile, and it does not require substrates nor products derivatization as opposed to common capillary electrophoresis methods used for glycosyltransferase activity measurements.
| Translated title of the contribution | Enzymatic assay of glycosyltransferases by capillary electrophoresis without derivatization |
|---|---|
| Original language | Spanish |
| Pages (from-to) | 356-363 |
| Number of pages | 8 |
| Journal | AFINIDAD |
| Volume | 64 |
| Issue number | 529 |
| Publication status | Published - 2007 May 1 |
| Externally published | Yes |
Free keywords
- Capillary electrophoresis
- Enzymatic activity
- Glycosyltransferases
- UDP