Purification and some properties of isocitrate dehydrogenase from Paracoccus denitrificans
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010270" target="_blank" >RIV/00216224:14310/04:00010270 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Purification and some properties of isocitrate dehydrogenase from Paracoccus denitrificans
Original language description
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.
Czech name
Purifikace a charakterizace isocitrátdehydrogenasy z Paracoccus denitrificans
Czech description
Purifikace a charakterizace isocitrátdehydrogenasy z Paracoccus denitrificans
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2004
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Preparative Biochemistry
ISSN
0032-7484
e-ISSN
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Volume of the periodical
34
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
279-289
UT code for WoS article
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EID of the result in the Scopus database
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