Účastní se degradace cytokininů v rostlinách fenolové látky?

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002097" target="_blank" >RIV/61989592:15310/04:00002097 - 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

Is the degradation of cytokinins in plants assisted by phenolics?

Popis výsledku v původním jazyce

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 1,2. Maize kernels 3 weeks after pollination and 2-week-old maize seedlings were examined. CKX activity was monitored using a spectrophotometric assay of the product aldehyde with 4-aminophenol3. Histochemical localization of CKX 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 4. CKX from maize showed the capability of using oxidation products of guaiacol, catechol, caffeic acid, acetosyringone, some flavonoids and several other compounds as electron acceptors. Further experiments revealed that the electron acceptors may be generated in vivo from plant phenolics by other enzymat

Název v anglickém jazyce

Is the degradation of cytokinins in plants assisted by phenolics?

Popis výsledku anglicky

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 1,2. Maize kernels 3 weeks after pollination and 2-week-old maize seedlings were examined. CKX activity was monitored using a spectrophotometric assay of the product aldehyde with 4-aminophenol3. Histochemical localization of CKX 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 4. CKX from maize showed the capability of using oxidation products of guaiacol, catechol, caffeic acid, acetosyringone, some flavonoids and several other compounds as electron acceptors. Further experiments revealed that the electron acceptors may be generated in vivo from plant phenolics by other enzymat

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 Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

S

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

49

Kód UT WoS článku

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EID výsledku v databázi Scopus

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