Cytokinin dehydrogenases from Arabidopsis thaliana.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002102" target="_blank" >RIV/61989592:15310/04:00002102 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Cytokinin dehydrogenases from Arabidopsis thaliana.
Original language description
The purification of plant cytokinin dehydrogenases (CKX, EC 1.5.99.12), key enzymes in cytokinin degradation, is a complicated task due to their low amount and presence of several enzyme variants in plant tissues. The aim of this study was to characterize CKX enzymes in leaf extracts of tobacco plants over-expressing individual A. thaliana enzymes and prepare Saccharomyces cerevisiae clones for production of recombinant proteins. Genome integrating vector pYESX was the most suitable for expression and purification of AtCKX2 that was secreted into the growth medium. Leaf extracts of tobacco plants expressing AtCKX2 and AtCKX4 showed high levels of CKX activity, while the activities in other transformants were low. Properties of individual CKXs will be discussed.
Czech name
Cytokinindehydrogenasy z Arabidopsis thaliana.
Czech description
Příspěvek se věnuje izolaci cytokinindehydrogenasy z Arabidopsis thaliana.
Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA522%2F03%2F0979" target="_blank" >GA522/03/0979: Organization of cytokinin dehydrogenase genes in cereals and mechanism of the catalytic reaction of cytokinin degradation</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
Conference Handbook, 18th International Conference on Plant Growth Substances
ISBN
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ISSN
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e-ISSN
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Number of pages
144
Pages from-to
117
Publisher name
IPGSA
Place of publication
Canberra, Australia
Event location
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Event date
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Type of event by nationality
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UT code for WoS article
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