Purification and some properties of isocitrate dehydrogenase from Paracoccus denitrificans
| Authors | |
|---|---|
| Year of publication | 2004 |
| Type | Article in Periodical |
| Magazine / Source | Preparative Biochemistry |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Isocitrate dehydrogenase; purification; Paracoccus denitrificans |
| 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. |
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