Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids

The measurement of respiratory chain enzyme activities is an integral part of basic research as well as for specialized examinations in clinical biochemistry. Most of the enzymes use ubiquinone as one of their substrates. For current in vitro measurements, several hydrophilic analogues of native ubi...

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Autores principales: Čermáková, Petra, Kovalinka, Tomáš, Ferenczyová, Kristína, Horváth, Anton
Formato: Online Artículo Texto
Lenguaje:English
Publicado: EDP Sciences 2019
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6430614/
https://www.ncbi.nlm.nih.gov/pubmed/30901308
http://dx.doi.org/10.1051/parasite/2019017
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author Čermáková, Petra
Kovalinka, Tomáš
Ferenczyová, Kristína
Horváth, Anton
author_facet Čermáková, Petra
Kovalinka, Tomáš
Ferenczyová, Kristína
Horváth, Anton
author_sort Čermáková, Petra
collection PubMed
description The measurement of respiratory chain enzyme activities is an integral part of basic research as well as for specialized examinations in clinical biochemistry. Most of the enzymes use ubiquinone as one of their substrates. For current in vitro measurements, several hydrophilic analogues of native ubiquinone are used depending on the enzyme and the workplace. We tested five readily available commercial analogues and we showed that Coenzyme Q(2) is the most suitable for the measurement of all tested enzyme activities. Use of a single substrate in all laboratories for several respiratory chain enzymes will improve our ability to compare data, in addition to simplifying the stock of chemicals required for this type of research.
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spelling pubmed-64306142019-04-17 Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids Čermáková, Petra Kovalinka, Tomáš Ferenczyová, Kristína Horváth, Anton Parasite Research Article The measurement of respiratory chain enzyme activities is an integral part of basic research as well as for specialized examinations in clinical biochemistry. Most of the enzymes use ubiquinone as one of their substrates. For current in vitro measurements, several hydrophilic analogues of native ubiquinone are used depending on the enzyme and the workplace. We tested five readily available commercial analogues and we showed that Coenzyme Q(2) is the most suitable for the measurement of all tested enzyme activities. Use of a single substrate in all laboratories for several respiratory chain enzymes will improve our ability to compare data, in addition to simplifying the stock of chemicals required for this type of research. EDP Sciences 2019-03-22 /pmc/articles/PMC6430614/ /pubmed/30901308 http://dx.doi.org/10.1051/parasite/2019017 Text en © P. Čermáková et al., published by EDP Sciences, 2019 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Čermáková, Petra
Kovalinka, Tomáš
Ferenczyová, Kristína
Horváth, Anton
Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
title Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
title_full Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
title_fullStr Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
title_full_unstemmed Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
title_short Coenzyme Q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
title_sort coenzyme q(2) is a universal substrate for the measurement of respiratory chain enzyme activities in trypanosomatids
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6430614/
https://www.ncbi.nlm.nih.gov/pubmed/30901308
http://dx.doi.org/10.1051/parasite/2019017
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