The metabolism of polyamine oxidation products in plants - characterisation of aminoaldehyde dehydrogenase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F00%3A00001155" target="_blank" >RIV/61989592:15310/00:00001155 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
The metabolism of polyamine oxidation products in plants - characterisation of aminoaldehyde dehydrogenase
Original language description
We developed first purification protocol enabling isolation of a homogeneous plant aminoaldehyde dehydrogenase (AMADH). AMADH was detected in polyacrylamide gels after native electrophoreses by means of an activity staining method with 3-aminopropionaldehyde as a substrate, based on the formation of a formazan dye by the reduction of nitroblue tetrazolium. Using the same staining technique, the ultrastructural localisation of AMADH was performed in etiolated pea seedlings.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/GA203%2F99%2FD048" target="_blank" >GA203/99/D048: Purification of plant aminoaldehyde dehydrogenase and its enzymological characterization</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2000
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Chemické listy
ISSN
0009-2770
e-ISSN
—
Volume of the periodical
94
Issue of the periodical within the volume
8
Country of publishing house
XX - stateless person
Number of pages
1
Pages from-to
—
UT code for WoS article
—
EID of the result in the Scopus database
—