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

Result code in 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>
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Xanthine dehydrogenase from pea seedlings: a member of plant molybdenum oxidoreductase family
Original language 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 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
Czech name
—
Czech description
—

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)