TY - JOUR
T1 - Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización
AU - Linares-Pastén, Javier A.
AU - Planas, Antoni
PY - 2007/5
Y1 - 2007/5
N2 - 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.
AB - 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.
KW - Capillary electrophoresis
KW - Enzymatic activity
KW - Glycosyltransferases
KW - UDP
UR - http://www.scopus.com/inward/record.url?scp=39149097504&partnerID=8YFLogxK
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=pure_univeritat_ramon_llull&SrcAuth=WosAPI&KeyUT=WOS:000253103700006&DestLinkType=FullRecord&DestApp=WOS
M3 - Artículo
AN - SCOPUS:39149097504
SN - 0001-9704
VL - 64
SP - 356
EP - 363
JO - Afinidad
JF - Afinidad
IS - 529
ER -