Caleosin z Arabidopsis thaliana: vliv vápníku na funkci a strukturu

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F08%3A00021235" target="_blank" >RIV/60461373:22330/08:00021235 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Caleosin of Arabidopsis thaliana: Effect of Calcium on Functional and Structural Properties

Popis výsledku v původním jazyce

A non-radioactive blot binding assay has proved the capacity of a purified recombinant form of Arabidopsis thaliana caleosin (AtClo1), a key protein of this plant oil body, to bind calcium. Calcium affected recombinant caleosin aggregation state, solubility, and electrophoretic mobility on SDS-PAGE. The effect of calcium on interfacial behavior of recombinant caleosin was studied at three interfaces: air/water (A/W), purified oil/water (O/W), and air/phosholipid/water (A/PLs/W). Recombinant caleosin wasable to decrease interfacial tension (IFT) at A/W and O/W interfaces as a function of concentration and calcium, whereas no interaction was detected at the A/PLs/W interface. Effect of calcium was time dependent, and its amplitude strongly varied with the interface considered. Reconstituted oil bodies were used to prove the involvement of recombinant caleosin in their calcium-driven aggregation and coalescence. Calcium ions at concentration as low as 100 nM were able to strongly modify

Název v anglickém jazyce

Caleosin of Arabidopsis thaliana: Effect of Calcium on Functional and Structural Properties

Popis výsledku anglicky

A non-radioactive blot binding assay has proved the capacity of a purified recombinant form of Arabidopsis thaliana caleosin (AtClo1), a key protein of this plant oil body, to bind calcium. Calcium affected recombinant caleosin aggregation state, solubility, and electrophoretic mobility on SDS-PAGE. The effect of calcium on interfacial behavior of recombinant caleosin was studied at three interfaces: air/water (A/W), purified oil/water (O/W), and air/phosholipid/water (A/PLs/W). Recombinant caleosin wasable to decrease interfacial tension (IFT) at A/W and O/W interfaces as a function of concentration and calcium, whereas no interaction was detected at the A/PLs/W interface. Effect of calcium was time dependent, and its amplitude strongly varied with the interface considered. Reconstituted oil bodies were used to prove the involvement of recombinant caleosin in their calcium-driven aggregation and coalescence. Calcium ions at concentration as low as 100 nM were able to strongly modify

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

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

Název periodika

Journal of Agricultural and Food Chemistry

ISSN

0021-8561

e-ISSN

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Svazek periodika

56

Číslo periodika v rámci svazku

23

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

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Kód UT WoS článku

000261429000022

EID výsledku v databázi Scopus

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