Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F11%3A00368595" target="_blank" >RIV/61389030:_____/11:00368595 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15310/11:10213118 RIV/61989592:15110/11:10213118

Výsledek na webu

<a href="http://dx.doi.org/10.1111/j.1439-0507.2010.01948.x" target="_blank" >http://dx.doi.org/10.1111/j.1439-0507.2010.01948.x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/j.1439-0507.2010.01948.x" target="_blank" >10.1111/j.1439-0507.2010.01948.x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes

Popis výsledku v původním jazyce

Cysteine dioxygenase (CDO, EC 1.13.11.20) catalyses the oxygenation of cysteine to cysteine sulphinic acid leading to the production of sulphite, sulphate and taurine as the final metabolites of cysteine catabolism. Keratinolytic fungi secrete sulphite and sulphate to reduce disulphide bridges in host tissue keratin proteins as the first step of keratinolysis. In the present study, we describe the identification of cDNA, as well as expression and characterisation of recombinant CDO protein from Trichophyton mentagrophytes. The cDNA was amplified using primers designed on the basis of high conservancy CDO regions identified in other fungi. PCR product was cloned and sequenced. Recombinant CDO was expressed in Escherichia colt, and affinity purified andidentified by matrix-assisted laser desorption/ionization - time-of-flight mass spectrometry (MALDI-TOF MS). Enzyme activity was assayed by monitoring the production of cysteine sulphinate using mass spectrometry.

Název v anglickém jazyce

Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes

Popis výsledku anglicky

Cysteine dioxygenase (CDO, EC 1.13.11.20) catalyses the oxygenation of cysteine to cysteine sulphinic acid leading to the production of sulphite, sulphate and taurine as the final metabolites of cysteine catabolism. Keratinolytic fungi secrete sulphite and sulphate to reduce disulphide bridges in host tissue keratin proteins as the first step of keratinolysis. In the present study, we describe the identification of cDNA, as well as expression and characterisation of recombinant CDO protein from Trichophyton mentagrophytes. The cDNA was amplified using primers designed on the basis of high conservancy CDO regions identified in other fungi. PCR product was cloned and sequenced. Recombinant CDO was expressed in Escherichia colt, and affinity purified andidentified by matrix-assisted laser desorption/ionization - time-of-flight mass spectrometry (MALDI-TOF MS). Enzyme activity was assayed by monitoring the production of cysteine sulphinate using mass spectrometry.

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/GA301%2F08%2F1649" target="_blank" >GA301/08/1649: Modulace buněčného dělení normálních a nádorových buněk inhibitory cyklin-dependentních kinas</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Mycoses

ISSN

0933-7407

e-ISSN

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Svazek periodika

54

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

7

Strana od-do

"E456"-"E462"

Kód UT WoS článku

000294878900118

EID výsledku v databázi Scopus

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