Comparison of Resins for Metal Oxide Affinity Chromatography with Mass Spectrometry Detection for the Determination of Phosphopeptides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11150%2F13%3A10139092" target="_blank" >RIV/00216208:11150/13:10139092 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60162694:G44__/13:43875028

Výsledek na webu

<a href="http://www.tandfonline.com/doi/abs/10.1080/00032719.2013.773437" target="_blank" >http://www.tandfonline.com/doi/abs/10.1080/00032719.2013.773437</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Comparison of Resins for Metal Oxide Affinity Chromatography with Mass Spectrometry Detection for the Determination of Phosphopeptides

Popis výsledku v původním jazyce

Protein phosphorylation is a crucial regulatory mechanism in majority of biological processes. During MS, there is a general need to diminish suppression effect of non-phosphorylated peptides and counterbalance low abundance and insufficient ionization of phosphopeptides. Therefore, selective enrichment of their content in complex mixture has become an indispensable part of any phosphoproteomic study. In this work we employed metal oxide affinity chromatography (MOAC) approach. We have compared classicapproach of mixing TiO2 and peptides in a microtube with microcolumns - commercial tips NuTips (TiO2/ZrO2 1:1) and TopTips (R) (TiO2, TiO2/ZrO2 1:1, and ZrO2). Selectivity of the given media towards phosphopeptides was tested on a tryptic digest of mixture of bovine proteins: /-casein and fetuin (phosphoproteins) with myoglobin and bovine serum albumin (non-phosphorylated proteins) in ratio 1:1:5:5 and 1:1:50:50, respectively. After enrichment, the obtained eluates were analyzed by tande

Název v anglickém jazyce

Comparison of Resins for Metal Oxide Affinity Chromatography with Mass Spectrometry Detection for the Determination of Phosphopeptides

Popis výsledku anglicky

Protein phosphorylation is a crucial regulatory mechanism in majority of biological processes. During MS, there is a general need to diminish suppression effect of non-phosphorylated peptides and counterbalance low abundance and insufficient ionization of phosphopeptides. Therefore, selective enrichment of their content in complex mixture has become an indispensable part of any phosphoproteomic study. In this work we employed metal oxide affinity chromatography (MOAC) approach. We have compared classicapproach of mixing TiO2 and peptides in a microtube with microcolumns - commercial tips NuTips (TiO2/ZrO2 1:1) and TopTips (R) (TiO2, TiO2/ZrO2 1:1, and ZrO2). Selectivity of the given media towards phosphopeptides was tested on a tryptic digest of mixture of bovine proteins: /-casein and fetuin (phosphoproteins) with myoglobin and bovine serum albumin (non-phosphorylated proteins) in ratio 1:1:5:5 and 1:1:50:50, respectively. After enrichment, the obtained eluates were analyzed by tande

Druh

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

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

<a href="/cs/project/GPP206%2F12%2FP338" target="_blank" >GPP206/12/P338: Analýza fosfoproteomu leukemických buněčných linií po ozáření.</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Analytical Letters

ISSN

0003-2719

e-ISSN

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Svazek periodika

46

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

20

Strana od-do

1505-1524

Kód UT WoS článku

000320084800004

EID výsledku v databázi Scopus

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