Příprava specifické protilátky proti aminoaldehyddehydrogenase a její použití pro mikroskopovou lokalizaci enzymu z hrachu

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Preparation of a specific anti-aminoaldehyde dehydrogenase antibody and its application for microscopic localisation of the enzyme from pea

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Preparation of a specific anti-aminoaldehyde dehydrogenase antibody and its application for microscopic localisation of the enzyme from pea

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

Suppl.

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

50-51

Kód UT WoS článku

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EID výsledku v databázi Scopus

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