J
2004
Purification and some properties of isocitrate dehydrogenase from Paracoccus denitrificans
JANICZEK, Oldřich, Zdeněk GLATZ, Michaela WIMMEROVÁ and Jitka PSOTOVÁ
Basic information
Original name
Purification and some properties of isocitrate dehydrogenase from Paracoccus denitrificans
Name in Czech
Purifikace a charakterizace isocitrátdehydrogenasy z Paracoccus denitrificans
Authors
JANICZEK, Oldřich (203 Czech Republic, guarantor),
Zdeněk GLATZ (203 Czech Republic),
Michaela WIMMEROVÁ (203 Czech Republic) and Jitka PSOTOVÁ (203 Czech Republic)
Edition
Preparative Biochemistry, New York, Marcel Dekker, Inc. 2004, 0032-7484
Other information
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14310/04:00010270
Organization unit
Faculty of Science
Keywords in English
Isocitrate dehydrogenase; purification; Paracoccus denitrificans
Tags
International impact, Reviewed
V originále
NADP-dependent isocitrate dehydrogenase (ICDH) from the bacterium Paracoccus denitrificans was purified to homogeneity. The purification procedure involved ammonium sulphate fractionation, ion exchange chromatography, and gel permeation chromatography. The purity of the enzyme was checked by polyacrylamide gel electrophoresis. ICDH is a dimer composed of two probably identical subunits of relative molecular weight 90000. The pH optimum of the enzyme reaction in the direction of substrate oxidation was found to be 5.6; the presence of Mn (2+) is essential for enzyme activity.
In Czech
Purifikace a charakterizace isocitrátdehydrogenasy z Paracoccus denitrificans
Links
| MSM 143100005, plan (intention) | | Name: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu | | Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Structure-function Relationships and their role in the Metabolism |
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