A novel approach for the determination of membrane protein expression levels based on LC-MS/MS

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F11%3A43891994" target="_blank" >RIV/60461373:22330/11:43891994 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61389030:_____/11:00365269 RIV/60076658:12310/11:43883064

Výsledek na webu

<a href="http://dx.doi.org/10.1080/10826076.2011.569808" target="_blank" >http://dx.doi.org/10.1080/10826076.2011.569808</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1080/10826076.2011.569808" target="_blank" >10.1080/10826076.2011.569808</a>

Jazyk výsledku

angličtina

Název v původním jazyce

A novel approach for the determination of membrane protein expression levels based on LC-MS/MS

Popis výsledku v původním jazyce

Membrane proteins play crucial roles in a number of cellular processes. Thus, the determination of their expression levels under various physiological conditions is crucial in many biological and biochemical studies. However, the extremely hydrophobic nature of proteins possessing transmembrane domains complicates their analysis. Therefore, we developed a new approach toward quantification of membrane proteins in complex mixtures combining reversed-phase chromatography on C4 resin and mass spectrometrictechniques using iTRAQ (Isobaric tags for relative and absolute quantitation) labels. Reversed-phase chromatography on C4 resin with stepwise elution with 2-propanol was used to reduce contamination with hydrophilic proteins and to fractionate membraneproteins according to their hydrophobicity. The method was tested on an artificially prepared defined ratio of plasma membrane proteins obtained from cell cultures of Arabidopsis thaliana by 2-phase partitioning of microsomal fractions. T

Název v anglickém jazyce

A novel approach for the determination of membrane protein expression levels based on LC-MS/MS

Popis výsledku anglicky

Membrane proteins play crucial roles in a number of cellular processes. Thus, the determination of their expression levels under various physiological conditions is crucial in many biological and biochemical studies. However, the extremely hydrophobic nature of proteins possessing transmembrane domains complicates their analysis. Therefore, we developed a new approach toward quantification of membrane proteins in complex mixtures combining reversed-phase chromatography on C4 resin and mass spectrometrictechniques using iTRAQ (Isobaric tags for relative and absolute quantitation) labels. Reversed-phase chromatography on C4 resin with stepwise elution with 2-propanol was used to reduce contamination with hydrophilic proteins and to fractionate membraneproteins according to their hydrophobicity. The method was tested on an artificially prepared defined ratio of plasma membrane proteins obtained from cell cultures of Arabidopsis thaliana by 2-phase partitioning of microsomal fractions. T

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Journal of Liquid Chromatography and Related Technologies

ISSN

1082-6076

e-ISSN

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Svazek periodika

34

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

1004-1013

Kód UT WoS článku

000291807100005

EID výsledku v databázi Scopus

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