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  • Metoda EMMA byla využita pro studium enzymove kinetiky enzymu fenolsulfotranferasy. (cs)
  • Electrophoretically mediated microanalysis (EMMA) was applied for the study of the kinetic parameters of the enzymatic reaction of phenol sulfotransferase SULT1A1 isoenzyme with 4-nitrophenol as a substrate. The SULT1A1 activity was determined by the quantitation of the product, 4-nitrophenyl sulfate, at 274 nm by using different injection and separation steps. This new approach solved the problem of the presence of the very strong inhibitor, adenosine 3',5'-bisphosphate (PAP), in the co-substrate solution (adenosine 3'-phosphate 5'-phosphosulfate, PAPS) which is unstable at room temperature. The inhibitor PAP was electrophoretically separated from the co-substrate PAPS before the injection of enzyme and substrate inside the capillary (and thus before their in-capillary encountering). With the developed in-capillary SULT1A1 activity assay an average Michaelis constant (Km) for 4-nitrophenol was calculated to be 0.84 M, a value which is consistent with a previously reported value. Strong substrate inhi
  • Electrophoretically mediated microanalysis (EMMA) was applied for the study of the kinetic parameters of the enzymatic reaction of phenol sulfotransferase SULT1A1 isoenzyme with 4-nitrophenol as a substrate. The SULT1A1 activity was determined by the quantitation of the product, 4-nitrophenyl sulfate, at 274 nm by using different injection and separation steps. This new approach solved the problem of the presence of the very strong inhibitor, adenosine 3',5'-bisphosphate (PAP), in the co-substrate solution (adenosine 3'-phosphate 5'-phosphosulfate, PAPS) which is unstable at room temperature. The inhibitor PAP was electrophoretically separated from the co-substrate PAPS before the injection of enzyme and substrate inside the capillary (and thus before their in-capillary encountering). With the developed in-capillary SULT1A1 activity assay an average Michaelis constant (Km) for 4-nitrophenol was calculated to be 0.84 M, a value which is consistent with a previously reported value. Strong substrate inhi (en)
Title
  • Studium enzymove kinetiky enzymu fenolsulfotranferasy metodou EMMA (cs)
  • Study of enzyme kinetics of phenol sulfotransferase by electrophoretically mediated microanalysis
  • Study of enzyme kinetics of phenol sulfotransferase by electrophoretically mediated microanalysis (en)
skos:prefLabel
  • Studium enzymove kinetiky enzymu fenolsulfotranferasy metodou EMMA (cs)
  • Study of enzyme kinetics of phenol sulfotransferase by electrophoretically mediated microanalysis
  • Study of enzyme kinetics of phenol sulfotransferase by electrophoretically mediated microanalysis (en)
skos:notation
  • RIV/00216224:14310/04:00009928!RIV09-GA0-14310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/03/1025), P(GA203/03/1125), Z(MSM 143100005)
http://linked.open...iv/cisloPeriodika
  • (1+2)
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
  • 588780
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/04:00009928
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Capillary electrophoresis; enzymes; EMMA; sulfotranferase (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [30E5698F3DF3]
http://linked.open...i/riv/nazevZdroje
  • Journal of Chromatography A
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...v/svazekPeriodika
  • 1032
http://linked.open...iv/tvurceVysledku
  • Glatz, Zdeněk
  • Vytisková, Soňa
  • Hoogmartens, Jos
  • Van Schepdael, Ann
  • Van Dyck, Sigrid
http://linked.open...n/vavai/riv/zamer
issn
  • 0021-9606
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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