Revealing phosphoproteins playing role in tobacco pollen activated in vitro

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F12%3A00384621" target="_blank" >RIV/61389030:_____/12:00384621 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/pmic.201100318" target="_blank" >http://dx.doi.org/10.1002/pmic.201100318</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/pmic.201100318" target="_blank" >10.1002/pmic.201100318</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Revealing phosphoproteins playing role in tobacco pollen activated in vitro

Popis výsledku v původním jazyce

The transition between the quiescent mature and the metabolically active germinating pollen grain most probably involves changes in protein phosphorylation status, since phosphorylation has been implicated in the regulation of many cellular processes. Given that, only a minor proportion of cellular proteins are phosphorylated at any one time, and that phosphorylated and nonphosphorylated forms of many proteins can co-exist within a cell, the identification of phosphoproteins requires some prior enrichment from a crude protein extract. Here, we have used metal oxide/hydroxide affinity chromatography (MOAC) based on an aluminum hydroxide matrix for this purpose, and have generated a population of phosphoprotein candidates from both mature and in vitro activated tobacco pollen grains. Both electrophoretic and nonelectrophoretic methods, allied to MS, were applied to these extracts to identify a set of 139 phosphoprotein candidates. In vitro phosphorylation was also used to validate the sp

Název v anglickém jazyce

Revealing phosphoproteins playing role in tobacco pollen activated in vitro

Popis výsledku anglicky

The transition between the quiescent mature and the metabolically active germinating pollen grain most probably involves changes in protein phosphorylation status, since phosphorylation has been implicated in the regulation of many cellular processes. Given that, only a minor proportion of cellular proteins are phosphorylated at any one time, and that phosphorylated and nonphosphorylated forms of many proteins can co-exist within a cell, the identification of phosphoproteins requires some prior enrichment from a crude protein extract. Here, we have used metal oxide/hydroxide affinity chromatography (MOAC) based on an aluminum hydroxide matrix for this purpose, and have generated a population of phosphoprotein candidates from both mature and in vitro activated tobacco pollen grains. Both electrophoretic and nonelectrophoretic methods, allied to MS, were applied to these extracts to identify a set of 139 phosphoprotein candidates. In vitro phosphorylation was also used to validate the sp

Druh

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

CEP obor

ED - Fyziologie

OECD FORD obor

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Projekt

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

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Proteomics

ISSN

1615-9853

e-ISSN

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Svazek periodika

12

Číslo periodika v rámci svazku

21

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

22

Strana od-do

3229-3250

Kód UT WoS článku

000310564100012

EID výsledku v databázi Scopus

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