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Updated: Apr 29, 2026
In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
Published on: January 5, 2016
A luciferase-based method for assay of 5'-adenylylsulfate reductase
Xiaoli Xiang1, Guangtang Pan2, Tingzhao Rong2
1Department of Plant Biology and Pathology, Rutgers University, New Brunswick, NJ 08901, USA; Institute of Maize Research, Key Laboratory of Biology and Genetic Improvement of Maize in the Southwest Region, Ministry of Agriculture, Sichuan Agricultural University, Chengdu 611130, China.
Abstract:
A luciferase-based method was developed for measurement of 5'-adenylylsulfate (APS) reductase (APR), an enzyme of the reductive sulfate assimilation pathway in prokaryotes and plants. APR catalyzes the two-electron reduction of APS and forms sulfite and adenosine 5'-monophospahate (AMP). The luciferase-based assay measures AMP production using an enzyme-coupled system that generates luminescence. The method is shown to provide an accurate measurement of APR kinetic properties and can be used for both endpoint and continuous assays. APR activity can be measured from pure enzyme preparations as well as from crude protein extracts of tissues. In addition, the assay is ideally suited to high-throughput sample analysis of APR activity in a microtiter dish format. The method adds new capability to the study of the biochemistry and physiology of APR.
