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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

  • DOI - Digital Object Identifier

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

Result continuities

  • Project

  • 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

  • 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

  • EID of the result in the Scopus database