Purifikace a charakterizace aminoxidasy a jejího endogenního inhibitoru z Phaseolus vulgaris.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F01%3A00002026" target="_blank" >RIV/61989592:15310/01:00002026 - 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

Purification and characterization of amine oxidase and its endogenous inhibitor from Phaseolus vulgaris

Popis výsledku v původním jazyce

Amine oxidase activity in the seedlings homogenates of common bean (Phaseolus vulgaris) was reported to be absent due to the presence of low-molecular endogenous inhibitor. We investigated the changes in amine oxidase activity in developing bean seedlings by the use of biosensor-immobilized tissue cuttings and by histochemical analysis. Amine oxidase was isolated and purified to apparent homogeneity from 5-days old etiolated seedlings. The isolation scheme included fractionation by ammonium sulphate, ion-exchange chromatography on DEAE-cellulose and hydrophobic chromatography on hydroxyapatite. Further purification was achieved through HPLC on ion-exchange and gel columns. Purified enzyme was characterised by native and SDS-electrophoresis. After native electrophoresis, the enzyme was transferred to cellulose acetate membranes by semi-dry blotting, but antibodies to amine oxidase from pea (Pisum sativum) did not show cross-reactivity with corresponding protein from Phaseolus. Spectrosc

Název v anglickém jazyce

Purification and characterization of amine oxidase and its endogenous inhibitor from Phaseolus vulgaris

Popis výsledku anglicky

Amine oxidase activity in the seedlings homogenates of common bean (Phaseolus vulgaris) was reported to be absent due to the presence of low-molecular endogenous inhibitor. We investigated the changes in amine oxidase activity in developing bean seedlings by the use of biosensor-immobilized tissue cuttings and by histochemical analysis. Amine oxidase was isolated and purified to apparent homogeneity from 5-days old etiolated seedlings. The isolation scheme included fractionation by ammonium sulphate, ion-exchange chromatography on DEAE-cellulose and hydrophobic chromatography on hydroxyapatite. Further purification was achieved through HPLC on ion-exchange and gel columns. Purified enzyme was characterised by native and SDS-electrophoresis. After native electrophoresis, the enzyme was transferred to cellulose acetate membranes by semi-dry blotting, but antibodies to amine oxidase from pea (Pisum sativum) did not show cross-reactivity with corresponding protein from Phaseolus. Spectrosc

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F00%2FD119" target="_blank" >GA203/00/D119: Studium struktury a vlastností endogenního inhibitoru aminoxidasy ze semenáčků fazolu a jeho analog</a><br>

Návaznosti

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

Rok uplatnění

2001

Kód důvěrnosti údajů

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

Název statě ve sborníku

Proceedings of 2nd International Symposium "Separations in the BioSciences - SBS 2001"

ISBN

80-7080-437-8

ISSN

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e-ISSN

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Počet stran výsledku

159

Strana od-do

122

Název nakladatele

Česká společnost chemická

Místo vydání

Praha

Místo konání akce

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Datum konání akce

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Typ akce podle státní příslušnosti

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Kód UT WoS článku

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