Affinity Capillary Electrophoresis Applied to Investigation of Valinomycin Complexes with Ammonium and Alkali Metal Ions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00467288" target="_blank" >RIV/61388963:_____/16:00467288 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1007/978-1-4939-4014-1_17" target="_blank" >http://dx.doi.org/10.1007/978-1-4939-4014-1_17</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/978-1-4939-4014-1_17" target="_blank" >10.1007/978-1-4939-4014-1_17</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Affinity Capillary Electrophoresis Applied to Investigation of Valinomycin Complexes with Ammonium and Alkali Metal Ions

Popis výsledku v původním jazyce

This chapter deals with the application of affinity capillary electrophoresis (ACE) to investigation of noncovalent interactions (complexes) of valinomycin, a macrocyclic dodecadepsipeptide antibiotic ionophore, with ammonium and alkali metal ions (lithium, sodium, potassium, rubidium, and cesium). The strength of these interactions was characterized by the apparent binding (stability, association) constants (K-b) of the above valinomycin complexes using the mobility shift assay mode of ACE. The study involved measurements of effective electrophoretic mobility of valinomycin at variable concentrations of ammonium or alkali metal ions in the background electrolyte (BGE). The effective electrophoretic mobilities of valinomycin measured at ambient temperature and variable ionic strength were first corrected to the reference temperature 25 degrees C and constant ionic strength (10 or 25 mM). Then, from the dependence of the corrected valinomycin effective mobility on the ammonium or alkali metal ion concentration in the BGE, the apparent binding constants of the valinomycin-ammonium or valinomycin-alkali metal ion complexes were determined using a nonlinear regression analysis. Logarithmic form of the binding constants (log Kb) were found to be in the range of 1.50-4.63, decreasing in the order Rb+ > K+ > Cs+ > > Na+ > NH4+ similar to Li+.

Název v anglickém jazyce

Affinity Capillary Electrophoresis Applied to Investigation of Valinomycin Complexes with Ammonium and Alkali Metal Ions

Popis výsledku anglicky

This chapter deals with the application of affinity capillary electrophoresis (ACE) to investigation of noncovalent interactions (complexes) of valinomycin, a macrocyclic dodecadepsipeptide antibiotic ionophore, with ammonium and alkali metal ions (lithium, sodium, potassium, rubidium, and cesium). The strength of these interactions was characterized by the apparent binding (stability, association) constants (K-b) of the above valinomycin complexes using the mobility shift assay mode of ACE. The study involved measurements of effective electrophoretic mobility of valinomycin at variable concentrations of ammonium or alkali metal ions in the background electrolyte (BGE). The effective electrophoretic mobilities of valinomycin measured at ambient temperature and variable ionic strength were first corrected to the reference temperature 25 degrees C and constant ionic strength (10 or 25 mM). Then, from the dependence of the corrected valinomycin effective mobility on the ammonium or alkali metal ion concentration in the BGE, the apparent binding constants of the valinomycin-ammonium or valinomycin-alkali metal ion complexes were determined using a nonlinear regression analysis. Logarithmic form of the binding constants (log Kb) were found to be in the range of 1.50-4.63, decreasing in the order Rb+ > K+ > Cs+ > > Na+ > NH4+ similar to Li+.

Druh

C - Kapitola v odborné knize

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název knihy nebo sborníku

Capillary Electrophoresis of Proteins and Peptides: Methods and Protocols

ISBN

978-1-4939-4012-7

Počet stran výsledku

14

Strana od-do

219-232

Počet stran knihy

234

Název nakladatele

Springer

Místo vydání

New York

Kód UT WoS kapitoly

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