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Description
| - 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)
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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)
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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)
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skos:notation
| - RIV/00216224:14310/04:00009928!RIV09-GA0-14310___
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - P(GA203/03/1025), P(GA203/03/1125), Z(MSM 143100005)
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/04:00009928
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - Capillary electrophoresis; enzymes; EMMA; sulfotranferase (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
| - Journal of Chromatography A
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Glatz, Zdeněk
- Vytisková, Soňa
- Hoogmartens, Jos
- Van Schepdael, Ann
- Van Dyck, Sigrid
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://localhost/t...ganizacniJednotka
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