Vidilaseris, K, Kellosalo, J and Goldman, A orcid.org/0000-0001-8032-9700 (2018) A high-throughput method for orthophosphate determination of thermostable membrane-bound pyrophosphatase activity. Analytical Methods, 10 (6). pp. 646-651. ISSN 1759-9660
Abstract
Membrane-bound pyrophosphatases (mPPases) are homodimeric integral membrane proteins that hydrolyse pyrophosphate into orthophosphates coupled to the active transport of protons or sodium ions across membranes. They occur in bacteria, archaea, plants, and protist parasites. As they are essential in protist parasites and there are no homologous proteins in animals and humans, these enzymes represent an excellent drug target for treating protistal diseases. Experimental screening to find drug candidates is an important step to discover new hit compounds. For that, a cheap, simple, and robust assay is needed. Here we report the application of the molybdenum blue reaction method for a medium throughput microplate activity assay of the hyperthermophilic bacterium Thermotoga maritima mPPase and the possible application of the assay to screen inhibitors of membrane-bound pyrophosphatases.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence [https://creativecommons.org/licenses/by-nc/3.0/] |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 27 Mar 2018 15:41 |
Last Modified: | 06 Jul 2018 10:14 |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/c7ay02558k |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:129017 |