The nature of carbon dioxide substrate and equilibrium constant of the 6-phosphogluconate dehydrogenase reaction
- 1 December 1969
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 115 (4) , 633-638
- https://doi.org/10.1042/bj1150633
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The redox state of free nicotinamide–adenine dinucleotide phosphate in the cytoplasm of rat liverBiochemical Journal, 1969
- Purification and properties of 6-phosphogluconate dehydrogenase from sheep liverBiochemical Journal, 1969
- The mechanisms of reductive carboxylation reactions. Carbon dioxide or bicarbonate as substrate of nicotinamide-adenine dinucleotide phosphate-linked isocitrate dehydrogenase and ‘malic’ enzymeBiochemical Journal, 1968
- The equilibrium constant of the isocitrate dehydrogenase reactionBiochemical Journal, 1968
- The equilibrium constants of the glutamate dehydrogenase systemsBiochemical Journal, 1967
- The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liverBiochemical Journal, 1967
- BIOLOGICAL OXIDATIONSAnnual Review of Biochemistry, 1960
- The oxidative pentose phosphate cycle. I. Preparation of substrates and enzymesArchives of Biochemistry and Biophysics, 1958
- The free-energy changes associated with the individual steps of the tricarboxylic acid cycle, glycolysis and alcoholic fermentation and with the hydrolysis of the pyrophosphate groups of adenosinetriphosphateBiochemical Journal, 1953
- A NEW SPECTROPHOTOMETRIC METHOD FOR THE DETECTION AND DETERMINATION OF KETO SUGARS AND TRIOSESJournal of Biological Chemistry, 1951