Physicochemical Properties of the Diphosphopyridine Nucleotide-specific Isocitrate Dehydrogenase of Pig Heart
Open Access
- 1 December 1974
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 249 (24), 7942-7949
- https://doi.org/10.1016/s0021-9258(19)42056-5
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Role of metal ions in reaction catalyzed by pig heart triphosphopyridine nucleotide-dependent isocitrate dehydrogenase. III. Frequency and temperature dependence of the proton relaxation rates of solvent and substrate interaction with isocitrate dehydrogenase-bound manganese(II)Biochemistry, 1974
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Kinetic aspects of conformational changes in proteins. I. Rate of regain of enzyme activity from denatured proteinsBiochemistry, 1971
- Kinetic aspects of conformational changes in proteins. II. Structural changes in renaturation of denatured proteinsBiochemistry, 1971
- Pig heart triphosphopyridine nucleotide specific isocitrate dehydrogenase. Single polypeptide chainBiochemistry, 1970
- Pyruvate carboxylase. XIII. Reversible inactivation by coldBiochemistry, 1969
- Characterization of the aggregated states of glycogen phosphorylases by gel electrophoresisBiochemistry, 1969
- Molecular sieve studies of interacting protein systems. V. Association of subunits of D-amino acid oxidase apoenzymeBiochemistry, 1969
- Deuterium solvent isotope effects in reactions catalyzed by isocitrate dehydrogenaseBiochemical and Biophysical Research Communications, 1969
- The separation of DPN-linked and TPN-linked isocitrate dehydrogenase activities of mammalian liverBiochemical and Biophysical Research Communications, 1967