BSA-Polysaccharide Interactions at Negatively Charged Electrode Surface. Effects of Current Density.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00511698" target="_blank" >RIV/68081707:_____/19:00511698 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/19:00113461

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/full/10.1002/elan.201900231" target="_blank" >https://onlinelibrary.wiley.com/doi/full/10.1002/elan.201900231</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/elan.201900231" target="_blank" >10.1002/elan.201900231</a>

Jazyk výsledku

angličtina

Název v původním jazyce

BSA-Polysaccharide Interactions at Negatively Charged Electrode Surface. Effects of Current Density.

Popis výsledku v původním jazyce

Constant current chronopotentiometric stripping (CPS) peak H due to catalytic hydrogen evolution reaction on Hg-containing electrodes appeared useful in the analysis of protein complexes with single-stranded and double-stranded DNA as well as with peptides. In dependence on stripping current (I-str), structural transition of the protein alone or in complexes can be followed as a result of the protein exposure to electric field effects. For the first time we show here that the CPS analysis can be used for the study of the interaction of BSA with a polysaccharide namely sodium alginate (SA). BSA-SA complex formation was accompanied by the shift of the structural transition of BSA to lowerI-str intensities. Another polysaccharide dextran did not alter I-str-dependent structural transition of BSA. BSA-SA complex can be disturbed by an electric field effect or high ionic strength confirming the electrostatic nature of BSA-SA interaction.

Název v anglickém jazyce

BSA-Polysaccharide Interactions at Negatively Charged Electrode Surface. Effects of Current Density.

Popis výsledku anglicky

Constant current chronopotentiometric stripping (CPS) peak H due to catalytic hydrogen evolution reaction on Hg-containing electrodes appeared useful in the analysis of protein complexes with single-stranded and double-stranded DNA as well as with peptides. In dependence on stripping current (I-str), structural transition of the protein alone or in complexes can be followed as a result of the protein exposure to electric field effects. For the first time we show here that the CPS analysis can be used for the study of the interaction of BSA with a polysaccharide namely sodium alginate (SA). BSA-SA complex formation was accompanied by the shift of the structural transition of BSA to lowerI-str intensities. Another polysaccharide dextran did not alter I-str-dependent structural transition of BSA. BSA-SA complex can be disturbed by an electric field effect or high ionic strength confirming the electrostatic nature of BSA-SA interaction.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Electroanalysis

ISSN

1040-0397

e-ISSN

—

Svazek periodika

31

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

5

Strana od-do

2007-2011

Kód UT WoS článku

000491476600021

EID výsledku v databázi Scopus

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