Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización

Javier A. Linares-Pastén; Antoni Planas

Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización

Ramon Llull University

Forskningsoutput: Tidskriftsbidrag › Artikel i vetenskaplig tidskrift › Peer review

Sammanfattning

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.

Bidragets översatta titel	Enzymatic assay of glycosyltransferases by capillary electrophoresis without derivatization
Originalspråk	spanska
Sidor (från-till)	356-363
Antal sidor	8
Tidskrift	AFINIDAD
Volym	64
Nummer	529
Status	Published - 2007 maj 1
Externt publicerad	Ja

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@article{48372122961c467bba372a508f2f8724,

title = "Ensayo enzim{\'a}tico de glicosiltransferasas mediante electroforesis capilar sin derivatizaci{\'o}n",

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.",

keywords = "Capillary electrophoresis, Enzymatic activity, Glycosyltransferases, UDP",

author = "Linares-Past{\'e}n, \{Javier A.\} and Antoni Planas",

year = "2007",

month = may,

day = "1",

language = "spanska",

volume = "64",

pages = "356--363",

journal = "AFINIDAD",

issn = "0001-9704",

publisher = "Asociacion de Quimicos del Instituto Quimico de Sarria",

number = "529",

}

TY - JOUR

T1 - Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización

AU - Linares-Pastén, Javier A.

AU - Planas, Antoni

PY - 2007/5/1

Y1 - 2007/5/1

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 - https://www.scopus.com/pages/publications/39149097504

M3 - Artikel i vetenskaplig tidskrift

AN - SCOPUS:39149097504

SN - 0001-9704

VL - 64

SP - 356

EP - 363

JO - AFINIDAD

JF - AFINIDAD

IS - 529

ER -

Ensayo enzimático de glicosiltransferasas mediante electroforesis capilar sin derivatización

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