Fenolové látky v rostlinách se zřejmě účastní katalytické reakce cytokinindehydrogenasy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002098" target="_blank" >RIV/61989592:15310/04:00002098 - 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

Possible involvement of plant phenolics in catalytic reaction of cytokinin dehydrogenase.

Popis výsledku v původním jazyce

Introduction: Degradation of cytokinins in plants is controlled by flavoprotein cytokinin dehydrogenase (CKX, EC 1.5.99.12). Cleavage of the cytokinin substrate proceeds via a ternary complex involving covalently bound FAD cofactor and a quinonic electron acceptor (Bilyeu etal., 2001; Frébortová etal., 2004).Material and Methods: Maize kernels 3 weeks after pollination and 2-week-old maize seedlings were examined. CKX activity was assayed according to Frébort etal., (2002). Histochemical localization ofCKX activity was done with PMS/NBT redox-dye system. Activity of laccase was stained with 3,3#-diaminobenzidine. Immunochemical detection of CKX protein was done using specific antibody against the enzyme from maize (Morris etal., 1999).Results and Conclusions: CKX from maize showed the capability of using electron acceptors that were oxidation products of guaiacol, catechol, caffeic acid, acetosyringone, some flavonoids and several other compounds. Further experiments revealed that suc

Název v anglickém jazyce

Possible involvement of plant phenolics in catalytic reaction of cytokinin dehydrogenase.

Popis výsledku anglicky

Introduction: Degradation of cytokinins in plants is controlled by flavoprotein cytokinin dehydrogenase (CKX, EC 1.5.99.12). Cleavage of the cytokinin substrate proceeds via a ternary complex involving covalently bound FAD cofactor and a quinonic electron acceptor (Bilyeu etal., 2001; Frébortová etal., 2004).Material and Methods: Maize kernels 3 weeks after pollination and 2-week-old maize seedlings were examined. CKX activity was assayed according to Frébort etal., (2002). Histochemical localization ofCKX activity was done with PMS/NBT redox-dye system. Activity of laccase was stained with 3,3#-diaminobenzidine. Immunochemical detection of CKX protein was done using specific antibody against the enzyme from maize (Morris etal., 1999).Results and Conclusions: CKX from maize showed the capability of using electron acceptors that were oxidation products of guaiacol, catechol, caffeic acid, acetosyringone, some flavonoids and several other compounds. Further experiments revealed that suc

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA522%2F03%2F0979" target="_blank" >GA522/03/0979: Organizace genů cytokinin dehydrogenázy v obilovinách a mechanismus katalytické reakce odbourávání cytokininů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název periodika

Acta Physiologiae Plantarum

ISSN

0137-5881

e-ISSN

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Svazek periodika

26

Číslo periodika v rámci svazku

S

Stát vydavatele periodika

PL - Polská republika

Počet stran výsledku

1

Strana od-do

38

Kód UT WoS článku

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EID výsledku v databázi Scopus

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