Purification of the Primary Dihydroorotate Dehydrogenase (Oxidase) from Rat Liver Mitochondria
- 31 December 1976
- journal article
- research article
- Published by Taylor & Francis in Preparative Biochemistry
- Vol. 7 (5), 345-355
- https://doi.org/10.1080/00327487708061654
Abstract
Dihydroorotate dehydrogenase was purified to homogeneity from rat liver mitochondria by Triton X-100 solubilization, diethylaminoethyl cellulose chromatography and gel electrophoresis. The overall yield was 30 percent. The enzyme has a subunit molecular weight of 61, 000.This publication has 8 references indexed in Scilit:
- Effects of chaotropic agents versus detergents on dihydroorotate dehydrogenase.Journal of Biological Chemistry, 1977
- Dihydroorotate-dependent superoxide producton in rat brain and liverArchives of Biochemistry and Biophysics, 1976
- Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acidJournal of Biological Chemistry, 1975
- A simple technique for eliminating interference by detergents in the Lowry method of protein determinationAnalytical Biochemistry, 1975
- Mammalian dihydroorotate – ubiquinone reductase complex. II. Correlation with cytochrome oxidase, mode of linkage with the cytochrome chain, and general propertiesCanadian Journal of Biochemistry, 1969
- [15] Isolation of liver or kidney mitochondriaPublished by Elsevier ,1967