About: Purification and characterization of ferric reductases from Paracoccus denitrificans     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)

AttributesValues
rdf:type
Description
  • Iron is a component of a number of biological systems, e.g. electron transport chains, cofactors of enzymes, regulatory proteins etc. It occurs in ferric form in environment, while organisms require ferrous iron. Enzymes catalysing the reduction of ferric complexes are widely spread within bacterial kingdom. Some of these enzymes are associated with cytoplasmic membrane, some are present in soluble form in cytoplasm or periplasm, some are excreted into extracellular medium. In our work, cellular fractions of Paracoccus denitrificans were tested for their activity towards reduction of various ferric complexes with NADH as an electron donor. We found the most of the ferric reductase activity in cytosolic fraction. Fe(III)-nitrilotriacetate was chosen as the best artificial substrate for activity measurements. Two proteins responsible for the activity was identified. Both enzymes were purified to homogeneity by combination of FPLC ion-exchange chromatography and chromatofocusing, and characterised with r
  • Iron is a component of a number of biological systems, e.g. electron transport chains, cofactors of enzymes, regulatory proteins etc. It occurs in ferric form in environment, while organisms require ferrous iron. Enzymes catalysing the reduction of ferric complexes are widely spread within bacterial kingdom. Some of these enzymes are associated with cytoplasmic membrane, some are present in soluble form in cytoplasm or periplasm, some are excreted into extracellular medium. In our work, cellular fractions of Paracoccus denitrificans were tested for their activity towards reduction of various ferric complexes with NADH as an electron donor. We found the most of the ferric reductase activity in cytosolic fraction. Fe(III)-nitrilotriacetate was chosen as the best artificial substrate for activity measurements. Two proteins responsible for the activity was identified. Both enzymes were purified to homogeneity by combination of FPLC ion-exchange chromatography and chromatofocusing, and characterised with r (en)
  • Iron is a component of a number of biological systems, e.g. electron transport chains, cofactors of enzymes, regulatory proteins etc. It occurs in ferric form in environment, while organisms require ferrous iron. Enzymes catalysing the reduction of ferric complexes are widely spread within bacterial kingdom. Some of these enzymes are associated with cytoplasmic membrane, some are present in soluble form in cytoplasm or periplasm, some are excreted into extracellular medium. In our work, cellular fractions of Paracoccus denitrificans were tested for their activity towards reduction of various ferric complexes with NADH as an electron donor. We found the most of the ferric reductase activity in cytosolic fraction. Fe(III)-nitrilotriacetate was chosen as the best artificial substrate for activity measurements. Two proteins responsible for the activity was identified. Both enzymes were purified to homogeneity by combination of FPLC ion-exchange chromatography and chromatofocusing, and characterised with r (cs)
Title
  • Purification and characterization of ferric reductases from Paracoccus denitrificans
  • Purification and characterization of ferric reductases from Paracoccus denitrificans (en)
  • Purification and characterization of ferric reductases from Paracoccus denitrificans (cs)
skos:prefLabel
  • Purification and characterization of ferric reductases from Paracoccus denitrificans
  • Purification and characterization of ferric reductases from Paracoccus denitrificans (en)
  • Purification and characterization of ferric reductases from Paracoccus denitrificans (cs)
skos:notation
  • RIV/00216224:14310/02:00006390!RIV08-GA0-14310___
http://linked.open.../vavai/riv/strany
  • 150
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/01/1589)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 661214
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/02:00006390
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • ferric reductase; Paracoccus denitrificans; purification (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [5FE8A5773F80]
http://linked.open...v/mistoKonaniAkce
  • 10.-13.9.2002 Stará Lesná, Slovenská republika
http://linked.open...i/riv/mistoVydani
  • Bratislava
http://linked.open...i/riv/nazevZdroje
  • XVIII. BIOCHEMICKÝ ZJAZD
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Kučera, Igor
  • Mazoch, Jiří
  • Turánek, Jaroslav
  • Tesařík, Radek
http://linked.open...vavai/riv/typAkce
http://linked.open.../riv/zahajeniAkce
number of pages
http://purl.org/ne...btex#hasPublisher
  • Slovenská spoločnosť pre biochémiu a molekulárnu biológiu pri SAV
http://localhost/t...ganizacniJednotka
  • 14310
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
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, 58 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software