Buněčná lokalizace a metabolické funkce aminoxidas indukovaných n-butylaminem v plísni Aspergillus niger AKU 3302

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F00%3A00000973" target="_blank" >RIV/61989592:15310/00:00000973 - 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

Cellular localization and metabolic function of n-butylamine induced amine oxidases in the fungus Aspergillus niger AKU 3302

Popis výsledku v původním jazyce

Using transmission electron microscopy, the amine oxidase activity in Aspergillus niger AKU 3302 was localized on the outer side of the cell wall but not inside the cell by cerium perhydroxide deposition method. Presence of cerium in the deposit was confirmed by energy dispersive microanalysis of X-rays. Interestingly, immunocytochemical localization using gold labeling with a specific antibody indicated the presence of amine oxidase protein inside the cell wall and not only on the outer surface. Besides the cell wall, high level of labeling was observed inside the cell in what seems to be secretory vesicle structures. It is proposed that the highly active amine oxidase AO-I is located in the cell wall to serve primarily as a detoxifying agent preventing amines from entering and damaging the cell. The amine oxidation exhibits an interesting spatial orientation involving a release of toxic hydrogen peroxide into extracellular space. On the other hand, the inactive amine oxidase protein

Název v anglickém jazyce

Cellular localization and metabolic function of n-butylamine induced amine oxidases in the fungus Aspergillus niger AKU 3302

Popis výsledku anglicky

Using transmission electron microscopy, the amine oxidase activity in Aspergillus niger AKU 3302 was localized on the outer side of the cell wall but not inside the cell by cerium perhydroxide deposition method. Presence of cerium in the deposit was confirmed by energy dispersive microanalysis of X-rays. Interestingly, immunocytochemical localization using gold labeling with a specific antibody indicated the presence of amine oxidase protein inside the cell wall and not only on the outer surface. Besides the cell wall, high level of labeling was observed inside the cell in what seems to be secretory vesicle structures. It is proposed that the highly active amine oxidase AO-I is located in the cell wall to serve primarily as a detoxifying agent preventing amines from entering and damaging the cell. The amine oxidation exhibits an interesting spatial orientation involving a release of toxic hydrogen peroxide into extracellular space. On the other hand, the inactive amine oxidase protein

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME%20153" target="_blank" >ME 153: Vlastnosti a využití enzymů oxidujících různé aminy s různými prostetickými skupinami z rostlin a mikroorganismů.</a><br>

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

Archives of Microbiology

ISSN

0302-8933

e-ISSN

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Svazek periodika

173

Číslo periodika v rámci svazku

5/6

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

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Kód UT WoS článku

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EID výsledku v databázi Scopus

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