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Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds

This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na(+),K(+)-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na(+),K(+)-ATPase, as well to preserve the enzyme properties were ove...

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Detalles Bibliográficos
Autores principales: Vasić, Vesna, Momić, Tatjana, Petković, Marijana, Krstić, Danijela
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791021/
https://www.ncbi.nlm.nih.gov/pubmed/27873990
http://dx.doi.org/10.3390/s8128321
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author Vasić, Vesna
Momić, Tatjana
Petković, Marijana
Krstić, Danijela
author_facet Vasić, Vesna
Momić, Tatjana
Petković, Marijana
Krstić, Danijela
author_sort Vasić, Vesna
collection PubMed
description This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na(+),K(+)-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na(+),K(+)-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na(+),K(+)-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research.
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spelling pubmed-37910212013-10-18 Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds Vasić, Vesna Momić, Tatjana Petković, Marijana Krstić, Danijela Sensors (Basel) Review This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na(+),K(+)-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na(+),K(+)-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na(+),K(+)-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research. Molecular Diversity Preservation International (MDPI) 2008-12-15 /pmc/articles/PMC3791021/ /pubmed/27873990 http://dx.doi.org/10.3390/s8128321 Text en © 2008 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 Review
Vasić, Vesna
Momić, Tatjana
Petković, Marijana
Krstić, Danijela
Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds
title Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds
title_full Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds
title_fullStr Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds
title_full_unstemmed Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds
title_short Na(+),K(+)-ATPase as the Target Enzyme for Organic and Inorganic Compounds
title_sort na(+),k(+)-atpase as the target enzyme for organic and inorganic compounds
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791021/
https://www.ncbi.nlm.nih.gov/pubmed/27873990
http://dx.doi.org/10.3390/s8128321
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