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A Modified Coupled Enzyme Method for O-linked GlcNAc Transferase Activity Assay

External protocol Created on 09 Apr 2014

Authors

Lianwen Zhang, Feifei Ren, Jing Li, Xiaofeng Ma, Peng Wang

Summary

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 diphosphate) (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 (E m = 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.

Further details

The protocol was imported from Springer Protocols. To see the entire protocol, click on the source link, or download the pdf here.

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