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Following Enzyme Activity with Infrared Spectroscopy
Fourier transform infrared (FTIR) spectroscopy provides a direct, “on-line” monitor of enzymatic reactions. Measurement of enzymatic activity is based on the fact that the infrared spectra of reactants and products of an enzymatic reaction are usually different. Several examples are given using the...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3274194/ https://www.ncbi.nlm.nih.gov/pubmed/22319264 http://dx.doi.org/10.3390/s100402626 |
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author | Kumar, Saroj Barth, Andreas |
author_facet | Kumar, Saroj Barth, Andreas |
author_sort | Kumar, Saroj |
collection | PubMed |
description | Fourier transform infrared (FTIR) spectroscopy provides a direct, “on-line” monitor of enzymatic reactions. Measurement of enzymatic activity is based on the fact that the infrared spectra of reactants and products of an enzymatic reaction are usually different. Several examples are given using the enzymes pyruvate kinase, fumarase and alcohol dehydrogenase. The main advantage of the infrared method is that it observes the reaction of interest directly, i.e., no activity assay is required to convert the progress of the reaction into an observable quantity. |
format | Online Article Text |
id | pubmed-3274194 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-32741942012-02-08 Following Enzyme Activity with Infrared Spectroscopy Kumar, Saroj Barth, Andreas Sensors (Basel) Article Fourier transform infrared (FTIR) spectroscopy provides a direct, “on-line” monitor of enzymatic reactions. Measurement of enzymatic activity is based on the fact that the infrared spectra of reactants and products of an enzymatic reaction are usually different. Several examples are given using the enzymes pyruvate kinase, fumarase and alcohol dehydrogenase. The main advantage of the infrared method is that it observes the reaction of interest directly, i.e., no activity assay is required to convert the progress of the reaction into an observable quantity. Molecular Diversity Preservation International (MDPI) 2010-03-25 /pmc/articles/PMC3274194/ /pubmed/22319264 http://dx.doi.org/10.3390/s100402626 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Kumar, Saroj Barth, Andreas Following Enzyme Activity with Infrared Spectroscopy |
title | Following Enzyme Activity with Infrared Spectroscopy |
title_full | Following Enzyme Activity with Infrared Spectroscopy |
title_fullStr | Following Enzyme Activity with Infrared Spectroscopy |
title_full_unstemmed | Following Enzyme Activity with Infrared Spectroscopy |
title_short | Following Enzyme Activity with Infrared Spectroscopy |
title_sort | following enzyme activity with infrared spectroscopy |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3274194/ https://www.ncbi.nlm.nih.gov/pubmed/22319264 http://dx.doi.org/10.3390/s100402626 |
work_keys_str_mv | AT kumarsaroj followingenzymeactivitywithinfraredspectroscopy AT barthandreas followingenzymeactivitywithinfraredspectroscopy |