All articles by Agnar P. Nygaard
20 articlesArticles in volume 8 (1954)
| Kinetics and Equilibria in Flavoprotein Systems. I. A Fluorescence Recorder and its Application to a Study of the Dissociation of the Old Yellow Enzyme and its Resynthesis from Riboflavine phosphate and Protein. Theorell, Hugo; Nygaard, Agnar P. Pages: 877-888. DOI number: 10.3891/acta.chem.scand.08-0877 |
| The Combination of Flavin Mononucleotide and Riboflavin with the Protein of "The Old Yellow Enzyme" Theorell, Hugo; Nygaard, Agnar P. Pages: 1104-1105. DOI number: 10.3891/acta.chem.scand.08-1104c |
| On the Chemical Nature of the FMN-Binding Groups in the Old Yellow Enzyme. Nygaard, Agnar P.; Theorell, Hugo Pages: 1489-1489. DOI number: 10.3891/acta.chem.scand.08-1489 |
| Kinetics of Alcohol Dehydrogenase, Studied with the Aid of a Fluorescence Recorder. Theorell, Hugo; Nygaard, Agnar P.; Bonnichsen, Roger Pages: 1490-1491. DOI number: 10.3891/acta.chem.scand.08-1490 |
| Kinetics and Equilibria in Flavoprotein Systems. II. The Effects of pH, Anions, and Temperature on the Dissociation and Reassociation of the Old Yellow Enzyme. Theorell, Hugo; Nygaard, Agnar P. Pages: 1649-1658. DOI number: 10.3891/acta.chem.scand.08-1649 |
Articles in volume 9 (1955)
| On the Chemical Nature of the FMN-binding Groups in the Old Yellow Enzyme. Nygaard, Agnar P.; Theorell, Hugo Pages: 202-202. DOI number: 10.3891/acta.chem.scand.09-0202c |
| Kinetics of Alcohol Dehydrogenases, Studied with the Aid of a Fluorescence Recorder. Theorell, Hugo; Nygaard, Agnar P.; Bonnichsen, Roger Pages: 202-202. DOI number: 10.3891/acta.chem.scand.09-0202a |
| On the Reactivity of Thiol Groups in Ox Heart Lactic Dehydrogenase. Pages: 1048-1048. DOI number: 10.3891/acta.chem.scand.09-1048 |
| Studies on Liver Alcohol Dehydrogenase. III. The Influence of pH and Some Anions on the Reaction Velocity Constants. Theorell, Hugo; Nygaard, Agnar P.; Bonnichsen, Roger Pages: 1148-1165. DOI number: 10.3891/acta.chem.scand.09-1148 |
| The Reaction Mechanism of Yeast Alcohol Dehydrogenase (ADH), Studied by Overall Reaction Velocities. Nygaard, Agnar P.; Theorell, Hugo Pages: 1300-1305. DOI number: 10.3891/acta.chem.scand.09-1300 |
| Dissociation Constants in the Yeast Alcohol Dehydrogenase System, Calculated from overall Reaction Velocities. Nygaard, Agnar P.; Theorell, Hugo Pages: 1551-1552. DOI number: 10.3891/acta.chem.scand.09-1551 |
| Kinetics and Equilibria in Flavoprotein Systems. III. The Effects of Chemical Modifications of the Apoprotein on the Dissociation and Reassociation of the Old Yellow Enzyme. Nygaard, Agnar P.; Theorell, Hugo Pages: 1587-1599. DOI number: 10.3891/acta.chem.scand.09-1587 |
Articles in volume 10 (1956)
| Interaction of Pyridine-Nucleotide linked Enzymes. Nygaard, Agnar P.; Rutter, William J. Pages: 37-48. DOI number: 10.3891/acta.chem.scand.10-0037 |
| Essential Groups in DPN-linked Lactic Dehydrogenase. Pages: 397-407. DOI number: 10.3891/acta.chem.scand.10-0397 |
| Reaction Velocities of DPN-linked Lactic Dehydrogenase. Pages: 408-412. DOI number: 10.3891/acta.chem.scand.10-0408 |
Articles in volume 11 (1957)
| Yeast Lactic Dehydrogenase. Pages: 1087-1087. DOI number: 10.3891/acta.chem.scand.11-1087b |
Articles in volume 12 (1958)
| Formation of Particulate Ribonucleoprotein with Enzymic Activities in vitro. Pages: 1697-1697. DOI number: 10.3891/acta.chem.scand.12-1697b |
Articles in volume 14 (1960)
| The Solubility and the Salt Sensitivity of Yeast D- and L- Lactic Cytochrome c Reductase. Pages: 229-229. DOI number: 10.3891/acta.chem.scand.14-0229 |
| Particulate and Soluble D-Lactic Cytochrome c Reductase of Yeast. Pages: 1843-1844. DOI number: 10.3891/acta.chem.scand.14-1843 |
Articles in volume 15 (1961)
| Reversible Transformation of the Acceptor Specificity of Yeast D-Lactic Cytochrome c Reductase. Pages: 1627-1628. DOI number: 10.3891/acta.chem.scand.15-1627 |