Physicochemical Properties of the Diphosphopyridine Nucleotide-specific Isocitrate Dehydrogenase of Pig Heart
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
1. The Enzymes, Vol. 7;Plaut,1963
2. Pig heart triphosphopyridine nucleotide specific isocitrate dehydrogenase. Single polypeptide chain
3. Substrate Independence of Molecular Weight of Triphosphopyridine Nucleotide-specific Isocitrate Dehydrogenase
4. Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii. Isolation and characterization
5. NADP-Linked Isocitrate Dehydrogenase from Beef Liver. Purification, Quaternary Structure and Catalytic Activity
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1. Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone reductase;Biochemical and Biophysical Research Communications;2008-12
2. Bovine NAD+-Dependent Isocitrate Dehydrogenase: Alternative Splicing and Tissue-Dependent Expression of Subunit 1;Biochemistry;2000-01-25
3. Identification of the Subunits and Target Peptides of Pig Heart NAD-Specific Isocitrate Dehydrogenase Modified by the Affinity Label 8-(4-Bromo-2,3-dioxobutylthio)NAD;Archives of Biochemistry and Biophysics;1997-12
4. Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-01
5. Unfolding and refolding of the NAD-dependent isocitrate dehydrogenase from yeast;International Journal of Biological Macromolecules;1993-04
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