Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F02%3A00001638" target="_blank" >RIV/61989592:15310/02:00001638 - 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

Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family

Popis výsledku v původním jazyce

Xanthine dehydrogenase (XDH, EC 1.1.1.204) was purified to homogeneity from etiolated pea (Pisum sativum conv. speciosum) seedlings. The procedure involved initial purification with precipitants followed by two low pressure chromatographic steps. The partially purified enzyme was further subjected to FPLC on Superdex and Uno Q columns and to affinity-interaction chromatography on Affi-Gel Blue. Purity of the final enzyme preparation was checked by SDS-PAGE. Pea XDH forms a dimer of 2 × 150 kDa in the native state and is an acidic protein with pI 5.3. The enzyme shows quite stringent substrate specificity; only xanthine and hypoxantine are oxidized at a high reaction rate, some aldehydes such as indole-3-acetaldehyde are converted as well, but at rateslower than 3%. The enzyme was strongly inhibited by allopurinol, a typical inhibitor of molybdenum cofactor-containing enzymes, and less strongly by adenine and some cytokinins with aromatic side chain. N-terminal amino acid sequence of t

Název v anglickém jazyce

Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family

Popis výsledku anglicky

Xanthine dehydrogenase (XDH, EC 1.1.1.204) was purified to homogeneity from etiolated pea (Pisum sativum conv. speciosum) seedlings. The procedure involved initial purification with precipitants followed by two low pressure chromatographic steps. The partially purified enzyme was further subjected to FPLC on Superdex and Uno Q columns and to affinity-interaction chromatography on Affi-Gel Blue. Purity of the final enzyme preparation was checked by SDS-PAGE. Pea XDH forms a dimer of 2 × 150 kDa in the native state and is an acidic protein with pI 5.3. The enzyme shows quite stringent substrate specificity; only xanthine and hypoxantine are oxidized at a high reaction rate, some aldehydes such as indole-3-acetaldehyde are converted as well, but at rateslower than 3%. The enzyme was strongly inhibited by allopurinol, a typical inhibitor of molybdenum cofactor-containing enzymes, and less strongly by adenine and some cytokinins with aromatic side chain. N-terminal amino acid sequence of 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

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2002

Kód důvěrnosti údajů

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

Název periodika

Plant Physiology and Biochemistry

ISSN

0981-9428

e-ISSN

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Svazek periodika

40

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

8

Strana od-do

393-400

Kód UT WoS článku

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EID výsledku v databázi Scopus

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