Activity of Na /K -activated Mg2 -dependent ATP-hydrolase in the cell-free extracts of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp Rod-9

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62157124%3A16370%2F15%3A43873469" target="_blank" >RIV/62157124:16370/15:43873469 - isvavai.cz</a>

Výsledek na webu

<a href="http://actavet.vfu.cz/84/1/0003/" target="_blank" >http://actavet.vfu.cz/84/1/0003/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2754/avb201585010003" target="_blank" >10.2754/avb201585010003</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Activity of Na /K -activated Mg2 -dependent ATP-hydrolase in the cell-free extracts of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp Rod-9

Popis výsledku v původním jazyce

The aim of our work was to study Na+/K+-activated Mg2+-dependent ATPase activity in cellfree extracts of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 isolated from the human large intestine, and to carry out the kinetic analysis of the enzyme reaction. The maximum ATPase activity for both bacterial strains at +35 oC was determined. The highest activities of the studied enzyme in the cell-free extracts of D. piger Vib-7 at pH 7.0 and Desulfomicrobium sp. Rod-9 at pH 6.5 were measured. Based on experimental data, the analysis of kinetic properties of the ATP-hydrolase reaction by the studied bacteria was carried out. The enzyme activity, initial (instantaneous) reaction rate (V0) and maximum rate of the ATPase reaction (Vmax) was significantly higher in D. piger Vib-7 cells than in Desulfomicrobium sp. Rod-9. Michaelis constants (Km) of the enzyme reaction for both bacterial strains were determined.

Název v anglickém jazyce

Activity of Na /K -activated Mg2 -dependent ATP-hydrolase in the cell-free extracts of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp Rod-9

Popis výsledku anglicky

The aim of our work was to study Na+/K+-activated Mg2+-dependent ATPase activity in cellfree extracts of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 isolated from the human large intestine, and to carry out the kinetic analysis of the enzyme reaction. The maximum ATPase activity for both bacterial strains at +35 oC was determined. The highest activities of the studied enzyme in the cell-free extracts of D. piger Vib-7 at pH 7.0 and Desulfomicrobium sp. Rod-9 at pH 6.5 were measured. Based on experimental data, the analysis of kinetic properties of the ATP-hydrolase reaction by the studied bacteria was carried out. The enzyme activity, initial (instantaneous) reaction rate (V0) and maximum rate of the ATPase reaction (Vmax) was significantly higher in D. piger Vib-7 cells than in Desulfomicrobium sp. Rod-9. Michaelis constants (Km) of the enzyme reaction for both bacterial strains were determined.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

30104 - Pharmacology and pharmacy

Projekt

<a href="/cs/project/EE2.3.30.0053" target="_blank" >EE2.3.30.0053: Farmakotoxikologické hodnocení nově syntetizovaných (izolovaných) látek jako nástroj integrace preklinických disciplín na VFU Brno</a><br>

Návaznosti

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

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Acta veterinaria Brno

ISSN

0001-7213

e-ISSN

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Svazek periodika

84

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

10

Strana od-do

3-12

Kód UT WoS článku

000351657800001

EID výsledku v databázi Scopus

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