A luciferase-based method for assay of 5′-adenylylsulfate reductase

Xiaoli Xiang, Guangtang Pan, Tingzhao Rong, Zhi Liang Zheng, Thomas Leustek

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)22-28
Number of pages7
JournalAnalytical Biochemistry
Volume460
DOIs
StatePublished - Sep 1 2014

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Keywords

  • Adenosine 5′-monophosphate
  • Adenosine 5′-phosphosulfate
  • Luciferase
  • Reductase
  • Sulfate assimilation

Fingerprint Dive into the research topics of 'A luciferase-based method for assay of 5′-adenylylsulfate reductase'. Together they form a unique fingerprint.

Cite this