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Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F02%3A00001638%21RIV%2F2003%2FMSM%2F153103%2FN
rdf:type
n10:Vysledek skos:Concept
dcterms:description
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 rates lower 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 the pea XDH shows 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 rates lower 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 the pea XDH shows
dcterms:title
Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family
skos:prefLabel
Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family
skos:notation
RIV/61989592:15310/02:00001638!RIV/2003/MSM/153103/N
n3:strany
393-400
n3:aktivita
n4:Z
n3:aktivity
Z(MSM 153100008), Z(MSM 153100010)
n3:cisloPeriodika
5
n3:dodaniDat
n7:2003
n3:domaciTvurceVysledku
n8:7890052 n8:4536274 n8:5433851 n8:5609763 n8:9708790
n3:druhVysledku
n16:J
n3:duvernostUdaju
n6:S
n3:entitaPredkladatele
n14:predkladatel
n3:idSjednocenehoVysledku
670853
n3:idVysledku
RIV/61989592:15310/02:00001638
n3:jazykVysledku
n15:eng
n3:klicovaSlova
Aldehyde oxidase; Molybdenum cofactor; Sequence; Pea; Purification; Xanthine dehydrogenase; Xanthine oxidase
n3:klicoveSlovo
n5:Xanthine%20oxidase n5:Sequence n5:Aldehyde%20oxidase n5:Xanthine%20dehydrogenase n5:Purification n5:Molybdenum%20cofactor n5:Pea
n3:kodStatuVydavatele
FR - Francouzská republika
n3:kontrolniKodProRIV
[E219ECAFD059]
n3:nazevZdroje
Plant Physiology and Biochemistry
n3:obor
n13:CE
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
7
n3:pocetUcastnikuAkce
0
n3:pocetZahranicnichUcastnikuAkce
0
n3:rokUplatneniVysledku
n7:2002
n3:svazekPeriodika
40
n3:tvurceVysledku
Peč, Pavel Frébort, Ivo Frébortová, Jitka Jacobsen, Susanne Šebela, Marek Galuszka, Petr Sauer, Pavel
n3:zamer
n18:MSM%20153100010 n18:MSM%20153100008
s:issn
0981-9428
s:numberOfPages
8
n17:organizacniJednotka
15310