Effect of His(6)-tagging of anterior gradient 2 protein on its electro-oxidation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F14%3A00440148" target="_blank" >RIV/68081707:_____/14:00440148 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00209805:_____/14:#0000567

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.electacta.2014.10.125" target="_blank" >http://dx.doi.org/10.1016/j.electacta.2014.10.125</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2014.10.125" target="_blank" >10.1016/j.electacta.2014.10.125</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Effect of His(6)-tagging of anterior gradient 2 protein on its electro-oxidation

Popis výsledku v původním jazyce

His-tagged and non-tagged forms of Anterior Gradient 2 (AGR2), oncoprotein and potential cancer biomarker, were studied for the first time using voltammetry at carbon electrodes. In addition to oxidation peak of Tyr and Trp, N-terminal His-tagged AGR2 form yielded characteristic electro-oxidation peak of histidine. Qualitatively similar results were obtained with other N-terminal His-tagged proteins, such as, glutathione-S-transferase, alpha-synuclein and cytochrome b5. Our results suggested that His-tag modification of proteins (commonly used in recombinant protein preparation) may change adsorption and orientation of the proteins at electrode surfaces. In absence of the His-tag in His-containing proteins, appearance of His peak was influenced by accessibility of His residues, and depended on the carbon electrode type. Oxidation His peak, in combination with Tyr and Trp oxidation responses may find use in label-free analysis of numerous proteins, including those important in biomedici

Název v anglickém jazyce

Effect of His(6)-tagging of anterior gradient 2 protein on its electro-oxidation

Popis výsledku anglicky

His-tagged and non-tagged forms of Anterior Gradient 2 (AGR2), oncoprotein and potential cancer biomarker, were studied for the first time using voltammetry at carbon electrodes. In addition to oxidation peak of Tyr and Trp, N-terminal His-tagged AGR2 form yielded characteristic electro-oxidation peak of histidine. Qualitatively similar results were obtained with other N-terminal His-tagged proteins, such as, glutathione-S-transferase, alpha-synuclein and cytochrome b5. Our results suggested that His-tag modification of proteins (commonly used in recombinant protein preparation) may change adsorption and orientation of the proteins at electrode surfaces. In absence of the His-tag in His-containing proteins, appearance of His peak was influenced by accessibility of His residues, and depended on the carbon electrode type. Oxidation His peak, in combination with Tyr and Trp oxidation responses may find use in label-free analysis of numerous proteins, including those important in biomedici

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

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

2014

Kód důvěrnosti údajů

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

Název periodika

Electrochimica acta

ISSN

0013-4686

e-ISSN

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Svazek periodika

150

Číslo periodika v rámci svazku

DEC2014

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

5

Strana od-do

218-222

Kód UT WoS článku

000346185000028

EID výsledku v databázi Scopus

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