Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización
Linares-Pastén, Javier A. LU
and Planas, Antoni
(2007)
In AFINIDAD
64(529).
p.356-363
- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/48372122-961c-467b-ba37-2a508f2f8724
- author
- Linares-Pastén, Javier A.
LU
and Planas, Antoni
- alternative title
- Enzymatic assay of glycosyltransferases by capillary electrophoresis without derivatization
- publishing date
- 2007-05-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Capillary electrophoresis, Enzymatic activity, Glycosyltransferases, UDP
- in
- AFINIDAD
- volume
- 64
- issue
- 529
- pages
- 8 pages
- publisher
- Asociacion de Quimicos del Instituto Quimico de Sarria
- external identifiers
-
- scopus:39149097504
- ISSN
- 0001-9704
- language
- Spanish
- LU publication?
- no
- id
- 48372122-961c-467b-ba37-2a508f2f8724
- date added to LUP
- 2018-10-09 01:34:06
- date last changed
- 2022-01-31 05:52:59
@article{48372122-961c-467b-ba37-2a508f2f8724,
abstract = {{<p>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.</p>}},
author = {{Linares-Pastén, Javier A. and Planas, Antoni}},
issn = {{0001-9704}},
keywords = {{Capillary electrophoresis; Enzymatic activity; Glycosyltransferases; UDP}},
language = {{spa}},
month = {{05}},
number = {{529}},
pages = {{356--363}},
publisher = {{Asociacion de Quimicos del Instituto Quimico de Sarria}},
series = {{AFINIDAD}},
title = {{Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización}},
volume = {{64}},
year = {{2007}},
}