Characterisation of a plant aminoaldehyde dehydrogenase

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F00%3A00001106" target="_blank" >RIV/61989592:15310/00:00001106 - 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

Characterisation of a plant aminoaldehyde dehydrogenase

Popis výsledku v původním jazyce

According to our knowledge, this is the first purification method developed, enabling isolation of a homogeneous aminoaldehyde dehydrogenase (AMADH) from etiolated pea seedlings. The procedure involved initial purification with precipitants followed by three low pressure chromatographic steps. Partially purified enzyme was further subjected to FPLC on a Mono Q column and to affinity-interaction chromatography on 5´-AMP Sepharose. Purity of the final enzyme preparation was checked by SDS-PAGE and chromatofocusing. Pea AMADH exists as a tetramer of 230 kDa in the native state, a molecular mass of one subunit was determined as 57 kDa. The enzyme was found to be an acidic protein with pI 5.4. AMADH showed a broad substrate specificity utilising various aminoaldehydes (C3-C6) as substrates. The best substrate of pea AMADH was 3-aminopropionaldehyde, the enzyme also efficiently oxidised 4-aminobutyraldehyde and w-guanidinoanalogues of the aminoaldehydes. Pea aminoaldehyde dehydrogenase was i

Název v anglickém jazyce

Characterisation of a plant aminoaldehyde dehydrogenase

Popis výsledku anglicky

According to our knowledge, this is the first purification method developed, enabling isolation of a homogeneous aminoaldehyde dehydrogenase (AMADH) from etiolated pea seedlings. The procedure involved initial purification with precipitants followed by three low pressure chromatographic steps. Partially purified enzyme was further subjected to FPLC on a Mono Q column and to affinity-interaction chromatography on 5´-AMP Sepharose. Purity of the final enzyme preparation was checked by SDS-PAGE and chromatofocusing. Pea AMADH exists as a tetramer of 230 kDa in the native state, a molecular mass of one subunit was determined as 57 kDa. The enzyme was found to be an acidic protein with pI 5.4. AMADH showed a broad substrate specificity utilising various aminoaldehydes (C3-C6) as substrates. The best substrate of pea AMADH was 3-aminopropionaldehyde, the enzyme also efficiently oxidised 4-aminobutyraldehyde and w-guanidinoanalogues of the aminoaldehydes. Pea aminoaldehyde dehydrogenase was i

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2000

Kód důvěrnosti údajů

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

Název periodika

Biochimica Et Biophysica Acta

ISSN

0006-3002

e-ISSN

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Svazek periodika

1480

Číslo periodika v rámci svazku

NA

Stát vydavatele periodika

XX - osoby bez státní příslušnosti

Počet stran výsledku

13

Strana od-do

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Kód UT WoS článku

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EID výsledku v databázi Scopus

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