J 2003

Inhibition study of rhodanese by means of electrophoretically mediated microanalysis

NOVÁKOVÁ, Soňa, Magdalena TELNAROVÁ and Zdeněk GLATZ

Basic information

Original name

Inhibition study of rhodanese by means of electrophoretically mediated microanalysis

Authors

NOVÁKOVÁ, Soňa (203 Czech Republic), Magdalena TELNAROVÁ (203 Czech Republic) and Zdeněk GLATZ (203 Czech Republic, guarantor)

Edition

Journal of Chromatography A, Netherlands, Elsevier, 2003, 0021-9606

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 2.950

RIV identification code

RIV/00216224:14310/03:00007945

Organization unit

Faculty of Science

UT WoS

000181647200021

Keywords in English

Capillary electrophoresis; Rhodenase; EMMA; Inhibition
Změněno: 19/5/2009 18:44, prof. RNDr. Zdeněk Glatz, CSc.

Abstract

V originále

A combination of the electrophoretically mediated microanalysis methodology with a partial filling technique was applied for the inhibition study of the bovine liver rhodanese by 2-oxoglutarate. In this set-up, the part of capillary is filled with the buffer best for the enzymatic reaction whereas, the rest of the capillary is filled with the background electrolyte optimal for separation of substrates and products. The estimated value of KI for 2-oxoglutarate was 3.62 x 10-4 ą 1.43 x 10-4 M with respect to cyanide and 1.40 x 10-3 ą 1.60 x 10-4 M with respect to thiosulfate. Moreover the type of inhibition was also evaluated. The findings of 2-oxogluatarate as the competitive inhibitor with respect to cyanide and as the uncompetitive inhibitor with respect to thiosulfate are in accordance with previous literature data.

Links

GA203/03/1125, research and development project
Name: Využití kapilární zónové elektroforézy pro studium enzymů
Investor: Czech Science Foundation, Application of capillary zone electrophoresis for the study of enzymes