Preparation of a specific anti-aminoaldehyde dehydrogenase antibody and its application for microscopic localisation of the enzyme from pea
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002056" target="_blank" >RIV/61989592:15310/04:00002056 - 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
Preparation of a specific anti-aminoaldehyde dehydrogenase antibody and its application for microscopic localisation of the enzyme from pea
Original language description
The studied enzyme - aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) from pea (Pisum sativum) - belongs to the group of NAD+-dependent dehydrogenases1. It catalyzes the oxidation of aminoaldehydes to the corresponding amino acids. It is involved in catabolic pathways of polyamines, which have been studied due to their regulatory properties in living organisms. Polyamines are oxidatively degraded by amine oxidases. There are two types of these enzymes: Cu-amine oxidases specific for diamines (DAO, EC 1.4.3.6.) and FAD-polyamine oxidases (PAO, EC 1.5.3.-.)2,3. Spermidine and spermine oxidation by PAO brings about the formation of 4-aminobutyraldehyde (ABAL) and N-(3-aminopropyl)-4-aminobutyraldehyde (APBAL), respectively, with the additional formation of 1,3-diaminopropane and H2O2. The diamines 1,3-diaminopropane and putrescine are converted to 3-aminopropionaldehyde (APAL) and ABAL, respectively. DAO participate in putrescine oxidation, however, the enzymatic system metabolising 1,3-d
Czech name
Příprava specifické protilátky proti aminoaldehyddehydrogenase a její použití pro mikroskopovou lokalizaci enzymu z hrachu
Czech description
Studie popisuje přípravu specifické protilátky proti aminoaldehyddehydrogenase a její použití pro mikroskopovou lokalizaci enzymu z hrachu.
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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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
Name of the periodical
Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
ISSN
0232-0061
e-ISSN
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Volume of the periodical
43
Issue of the periodical within the volume
Suppl.
Country of publishing house
CZ - CZECH REPUBLIC
Number of pages
275
Pages from-to
50-51
UT code for WoS article
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EID of the result in the Scopus database
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