About: Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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 coli, and affinity purified and identified 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. 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 coli, and affinity purified and identified 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. (en)
Title	Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes (en)
skos:prefLabel	Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes Isolation of recombinant cysteine dioxygenase protein from Trichophyton mentagrophytes (en)
skos:notation	RIV/61989592:15110/11:10213118!RIV14-GA0-15110___
http://linked.open...avai/predkladatel	Lékařská fakulta
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA301/08/1649), Z(AV0Z50380511), Z(MSM6198959216), Z(MSM6198959223)
http://linked.open...iv/cisloPeriodika	5
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	RAŠKA, Milan Kašperová, Alena Weigl, Evžen Horynová, Milada
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Lékařská fakulta
http://linked.open...dnocenehoVysledku	205924
http://linked.open...ai/riv/idVysledku	RIV/61989592:15110/11:10213118
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Trichophyton mentagrophytes; Recombinant cysteine dioxygenase (en)
http://linked.open.../riv/klicoveSlovo	Recombinant cysteine dioxygenase Trichophyton mentagrophytes
http://linked.open...odStatuVydavatele	DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV	[749D483F5AF1]
http://linked.open...i/riv/nazevZdroje	Mycoses
http://linked.open...in/vavai/riv/obor	EC
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Modulation of cell division of normal and cancer cells by cyclin-dependent kinase inhibitors
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	54
http://linked.open...iv/tvurceVysledku	Šebela, Marek Lenobel, René Raška, Milan Horynová, Milada Kašperová, Alena Kunert, Jiří Weigl, Evžen
http://linked.open...ain/vavai/riv/wos	000294878900118
http://linked.open...n/vavai/riv/zamer	Mechanismy regulace růstu a vývoje rostlin na úrovni buněk, orgánů a celých organismů: fyziologické, genetické a molekulárně biologické základy Modulation of signalling and regulatory pathways in normal and cancer cells Nové možnosti diagnostiky a imunomodulace u infekčních onemocnění a imunopatologických stavů
issn	0933-7407
number of pages	7 (xsd:int)
http://bibframe.org/vocab/doi	10.1111/j.1439-0507.2010.01948.x
http://localhost/t...ganizacniJednotka	15110

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 77 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software