Studium enzymových reakcí metodou EMMA v částečně plněné kapiláře s přímou nebo nepřímou detekcí.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00009907" target="_blank" >RIV/00216224:14310/04:00009907 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Study of Enzymatic Reaction by EMMA in a Partially Filled Capillary and Indirect or Direct Detection

Popis výsledku v původním jazyce

This report describes the application of electrophoretically mediated microanalysis (EMMA) in combination with a partial filling technique and indirect or direct detection for the study of enzymes dealing with the high mobile inorganic or organic anionsas substrates or products. In this set-up the part of the capillary is filled with the buffer best for the enzymatic reaction whereas the rest of the capillary with the background electrolyte optimal for separation of substrates and products. In the caseof haloalkane dehalogenase, which was chosen as a model enzyme, the enzymatic reaction was performed in 20 mM glycine buffer (pH 8.6). Because of wide substrate specifity of the enzyme, it utilizes chlorinated as well as brominated substrates producingeither non-absorbing chloride, or absorbing bromide ions, two different background electrolytes and the detection approaches were applied. A 10 mM chromate - 0.1 mM cetyltrimethylammonium bromide (pH 9.2) was used in combination with indi

Název v anglickém jazyce

Study of Enzymatic Reaction by EMMA in a Partially Filled Capillary and Indirect or Direct Detection

Popis výsledku anglicky

This report describes the application of electrophoretically mediated microanalysis (EMMA) in combination with a partial filling technique and indirect or direct detection for the study of enzymes dealing with the high mobile inorganic or organic anionsas substrates or products. In this set-up the part of the capillary is filled with the buffer best for the enzymatic reaction whereas the rest of the capillary with the background electrolyte optimal for separation of substrates and products. In the caseof haloalkane dehalogenase, which was chosen as a model enzyme, the enzymatic reaction was performed in 20 mM glycine buffer (pH 8.6). Because of wide substrate specifity of the enzyme, it utilizes chlorinated as well as brominated substrates producingeither non-absorbing chloride, or absorbing bromide ions, two different background electrolytes and the detection approaches were applied. A 10 mM chromate - 0.1 mM cetyltrimethylammonium bromide (pH 9.2) was used in combination with indi

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název periodika

Electrophoresis

ISSN

0173-0835

e-ISSN

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Svazek periodika

25

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

290-298

Kód UT WoS článku

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EID výsledku v databázi Scopus

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