原创力文档a modified coupled enzyme method for o-linked glcnac transferase activity assay改良酶耦合方法o-linked glcnac转移酶活力测定.pdfVIP
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a modified coupled enzyme method for o-linked glcnac transferase activity assay改良酶耦合方法o-linked glcnac转移酶活力测定
A Modified Coupled Enzyme Method for O-linked GlcNAc
Transferase Activity Assay
Lianwen Zhang, Feifei Ren, Jing Li, Xiaofeng Ma, and Peng Wang
Abstract
In order to determine the activity of O-linked GlcNAc transferase (OGT), a modified coupled enzyme
method was proposed. This method was based on the measurement of uridine 5′-(trihydrogen diphos-
phate) (UDP), a product generated in transglycosylation reaction. In the assay, UDP was coupled to
the conversion of phosphoenolpyruvate to pyruvate using pyruvate kinase. Using a commercial pyruvate
assay kit, the pyruvate was converted to a red terminal product, which could be photometrically measured
at 570 nm or fluorometrically measured at 587 nm (Em =535 nm) on a microplate reader. Kinetic study of
a truncated recombinant mOGT and quantitative analysis of OGT in two biological samples indicated
that this method was practical and competitive for quantitative analysis of OGT.
Keyword: O-linked GlcNAc transferase (OGT), coupled enzyme method, MS-glycosylation assay,
kinetic study.
Abbreviations
WGA-Agarose Agarose wheat germ agglutinin
FRET Fluorescence resonance energy transfer
PEP-K Mono-potassium phosphoenolpyruvate
OGT O-linked N-acetylglucosaminyltransferase
PK Pyruvate kinase
TPR Tetratricopeptide repeat
UDP Uridine 5′-(trihydrogen diphosphate)
IPTG Isopropyl β-D-thiogalactoside
Shulin Li (ed.), Biological Procedures Online, Volume 11, Number 1
© to the author(s) 2009
DOI: 10.1007/s12575-009-9016-x URL: ;
170
A Modified
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