All articles by Nils Ellfolk
53 articlesArticles in volume 4 (1950)
Oxidative Nitrogen Fixation in Ultrasonic Field. Virtanen, Artturi I.; Ellfolk, Nils Pages: 93-102. DOI number: 10.3891/acta.chem.scand.04-0093 |
Electrophoresis of Leghemoglobin. Ellfolk, Nils; Virtanen, Artturi I. Pages: 1014-1019. DOI number: 10.3891/acta.chem.scand.04-1014 |
Articles in volume 6 (1952)
The Molecular Weight of Leghemoglobin. Ellfolk, Nils; Virtanen, Artturi I. Pages: 411-420. DOI number: 10.3891/acta.chem.scand.06-0411 |
Inhibition of Oxidative Nitrogen Fixation in Ultrasonic Field by Volatile Substances. Virtanen, Artturi I.; Ellfolk, Nils Pages: 660-666. DOI number: 10.3891/acta.chem.scand.06-0660 |
Articles in volume 7 (1953)
Studies on Aspartase. I. Quantitative Separation of Aspartase from Bacterial Cells and Its Partial Purification. Pages: 824-830. DOI number: 10.3891/acta.chem.scand.07-0824 |
Studies on Aspartase. II. On the Chemical Nature of Aspartase. Pages: 1155-1163. DOI number: 10.3891/acta.chem.scand.07-1155 |
Articles in volume 8 (1954)
Studies on Aspartase. III. On the Specificity of Aspartase. Pages: 151-156. DOI number: 10.3891/acta.chem.scand.08-0151 |
Studies on Aspartase. IV. Effect of pH on Aspartase. Pages: 443-448. DOI number: 10.3891/acta.chem.scand.08-0443 |
Articles in volume 9 (1955)
Studies on Aspartase. V. Inactivation and Reactivation of Aspartase. Pages: 771-780. DOI number: 10.3891/acta.chem.scand.09-0771 |
Articles in volume 11 (1957)
The Effect of Volatile Substances on the Chemical Activity of Ultrasonic Cavitation. Ellfolk, Nils; Virtanen, Artturi I. Pages: 230-234. DOI number: 10.3891/acta.chem.scand.11-0230 |
Fractionation of Casein by Distribution in a Liquid Two-Phase System. Pages: 1317-1322. DOI number: 10.3891/acta.chem.scand.11-1317 |
Articles in volume 13 (1959)
Crystalline Leghemoglobin. Pages: 596-597. DOI number: 10.3891/acta.chem.scand.13-0596 |
Articles in volume 14 (1960)
Crystalline Leghemoglobin. 1. Purification Procedure. Pages: 609-616. DOI number: 10.3891/acta.chem.scand.14-0609 |
Crystalline Leghemoglobin. II.The Molecular Weights and Shapes of the two Main Components. Pages: 1819-1827. DOI number: 10.3891/acta.chem.scand.14-1819 |
Articles in volume 15 (1961)
Crystalline Leghemoglobin. V. The N-Terminal Amino Acids of the Two Main Components. Pages: 444-445. DOI number: 10.3891/acta.chem.scand.15-0444 |
Crystalline Leghemoglobin. III. Amino Acid Composition of the Two Main Components. Pages: 545-554. DOI number: 10.3891/acta.chem.scand.15-0545 |
Crystalline Leghemoglobin. IV. Spectroscopic Studies of the Two Main Metleghemoglobin Components and Some of their Fatty Acid Complexes. Pages: 975-984. DOI number: 10.3891/acta.chem.scand.15-0975 |
Articles in volume 16 (1962)
Crystalline Leghemoglobin. VI. The Comparison of the Two Main Components by Tryptic Peptide Pattern Analysis. Pages: 831-836. DOI number: 10.3891/acta.chem.scand.16-0831 |
Articles in volume 20 (1966)
Crystalline Cytochrome c Peroxidase. Pages: 1427-1428. DOI number: 10.3891/acta.chem.scand.20-1427 |
Articles in volume 21 (1967)
Cytochrome c Peroxidase. 1. Preparation of the Crystalline Enzyme from Baker's Yeast. Pages: 175-181. DOI number: 10.3891/acta.chem.scand.21-0175 |
Crystalline Leghemoglobin. X. The Ferrihemochrome of Leghemoglobin. Ellfolk, Nils; Sievers, Gunnel Pages: 1457-1461. DOI number: 10.3891/acta.chem.scand.21-1457 |
Cytochrome c Peroxidase. 2. The Size and Shape of Cytochrome c Peroxidase of Baker's Yeast. Pages: 1921-1924. DOI number: 10.3891/acta.chem.scand.21-1921 |
Cytochrome c Perioxidase. 3. The Amino Acid Composition of Cytochrome c Peroxidase of Baker's Yeast. Pages: 2736-2742. DOI number: 10.3891/acta.chem.scand.21-2736 |
Articles in volume 23 (1969)
Separation of Porphyrins by Multiple Liquid-Liquid Partition. Ellfolk, Nils; Hynninen, Paavo; Sievers, Gunnel Pages: 846-858. DOI number: 10.3891/acta.chem.scand.23-0846 |
Cytochrome c Peroxidase. IV. Isoelectric Focusing and Analysis of the Crystalline Enzyme in an Acidic pH Gradient. Ellfolk, Nils; Sievers, Gunnel Pages: 2550-2551. DOI number: 10.3891/acta.chem.scand.23-2550 |
Crystalline Leghemoglobin. XI. The Amino Acid Sequences of two Histidine-containing Tryptic Peptides of the Slow Component. Ellfolk, Nils; Sievers, Gunnel Pages: 2994-3002. DOI number: 10.3891/acta.chem.scand.23-2994 |
Articles in volume 24 (1970)
Crystalline Leghemoglobin. XII. A Spectrophotometric Study of the Slow Component in the Acid pH Range. Sievers, Gunnel; Ellfolk, Nils Pages: 439-444. DOI number: 10.3891/acta.chem.scand.24-0439 |
Pseudomonas Cytochrome c Peroxidase. I. Purification Procedure. Ellfolk, Nils; Soininen, Ritva Pages: 2126-2136. DOI number: 10.3891/acta.chem.scand.24-2126 |
Pseudomonas Cytochrome c Peroxidase. II. Localization of Cytochrome c Peroxidase in Pseudomonas fluorescens. Soininen, Ritva; Sojonen, Helinä; Ellfolk, Nils Pages: 2314-2320. DOI number: 10.3891/acta.chem.scand.24-2314 |
Articles in volume 25 (1971)
Crystalline Leghemoglobin. XIII. Sedimentation Studies. Behlke, Joachim; Sievers, Gunnel; Ellfolk, Nils Pages: 746-747. DOI number: 10.3891/acta.chem.scand.25-0746 |
Pseudomonas Cytochrome c Peroxidase. III. The Size and Shape of the Enzyme Molecule. Ellfolk, Nils; Soininen, Ritva Pages: 1535-1540. DOI number: 10.3891/acta.chem.scand.25-1535 |
The Primary Structure of Soybean Leghemoglobin. Ellfolk, Nils; Sievers, Gunnel Pages: 3532-3534. DOI number: 10.3891/acta.chem.scand.25-3532 |
Articles in volume 26 (1972)
Pseudomonas Cytochrome c Peroxidase. IV. Some Kinetic Properties of the Peroxidation Reaction, and Enzymatic Determination of the Extinction Coefficients of Pseudomonas Cytochrome c-551 and Azurin. Soininen, Ritva; Ellfolk, Nils Pages: 861-872. DOI number: 10.3891/acta.chem.scand.26-0861 |
The Primary Structure of Soybean Leghemoglobin. I. The Separation of the Tryptic Peptides of the Apoprotein from the Slow Component and Their Amino Acid Compositions. Ellfolk, Nils; Sievers, Gunnel Pages: 1155-1165. DOI number: 10.3891/acta.chem.scand.26-1155 |
Articles in volume 27 (1973)
Pseudomonas Cytochrome c Peroxidase. V. Absorption Spectra of the Enzyme and of its Compounds with Ligands. Inhibition of the Enzyme by Cyanide and Azide. Soininen, Ritva; Ellfolk, Nils Pages: 35-46. DOI number: 10.3891/acta.chem.scand.27-0035 |
Pseudomonas Cytochrome c Peroxidase. IX. Molecular Weight of the Enzyme in Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis. Soininen, Ritva; Ellfolk, Nils; Kalkkinen, Nisse Pages: 1106-1107. DOI number: 10.3891/acta.chem.scand.27-1106 |
Chlorophylls. I. Separation and Isolation of Chlorophylls a and b by Multiple Liquid-Liquid Partition. Hynninen, Paavo H.; Ellfolk, Nils Pages: 1463-1477. DOI number: 10.3891/acta.chem.scand.27-1463 |
Use of the Aqueous Formic Acid-Chloroform-Dimethylformamide Solvent System for the Purification of Porphyrins and Hemins. Hynninen, Paavo H.; Ellfolk, Nils Pages: 1795-1806. DOI number: 10.3891/acta.chem.scand.27-1795 |
Pseudomonas Cytochrome c Peroxidase. VII. Kinetics of the Peroxidatic Reaction Mechanism. Ellfolk, Nils; Rönnberg, Marjaana; Soininen, Ritva Pages: 2171-2178. DOI number: 10.3891/acta.chem.scand.27-2171 |
Pseudomonas Cytochrome c Peroxidase. VIII. The Amino Acid Composition of the Enzyme. Soininen, Ritva; Ellfolk, Nils Pages: 2193-2198. DOI number: 10.3891/acta.chem.scand.27-2193 |
The Primary Structure of Soybean Leghemoglobin. II. Amino Acid Sequence of Seventeen Peptides Isolated from the Tryptic Hydrolysate of the Slow Component. Ellfolk, Nils; Sievers, Gunnel Pages: 3371-3387. DOI number: 10.3891/acta.chem.scand.27-3371 |
Crystalline Leghemoglobin. XIV. Transfer of Hematin from Lba and Lbc to Horse-radish Peroxidase Apoprotein. Ellfolk, Nils; Pertilä, Ulla; Sievers, Gunnel Pages: 3601-3602. DOI number: 10.3891/acta.chem.scand.27-3601 |
The Primary Structure of Soybean Leghemoglobin. III. Fractionation and Sequence of Chymotryptic Peptides of the Apoprotein of the Slow Component. Ellfolk, Nils; Sievers, Gunnel Pages: 3817-3831. DOI number: 10.3891/acta.chem.scand.27-3817 |
The Primary Structure of Soybean Leghemoglobin. IV. Fractionation and Sequence of Thermolytic Peptides of the Apoprotein of the Slow Component (Lba). Ellfolk, Nils; Sievers, Gunnel Pages: 3986-3992. DOI number: 10.3891/acta.chem.scand.27-3986 |
Articles in volume 28b (1974)
Crystalline Leghemoglobin. XV. Effect of Urea on the Conformation of the Slow Component (Lba). Ellfolk, Nils; Sievers, Gunnel; Harmoinen, Aimo Pages: 1195-1199. DOI number: 10.3891/acta.chem.scand.28b-1195 |
Correction of the Amino Acid Sequence of Soybean Leghemoglobin a. Ellfolk, Nils; Sievers, Gunnel Pages: 1245-1246. DOI number: 10.3891/acta.chem.scand.28b-1245 |
Articles in volume 29b (1975)
Purification and Properties of Phaseolus vulgaris Leghemoglobin (PhLb). Lehtovaara, Päivi; Ellfolk, Nils Pages: 56-60. DOI number: 10.3891/acta.chem.scand.29b-0056 |
Pseudomonas Cytochrome c Peroxidase. X. The Effect of Pseudomonas Neutral Proteinase on the Enzyme Molecule. Soininen, Ritva; Ellfolk, Nils Pages: 134-136. DOI number: 10.3891/acta.chem.scand.29b-0134 |
Pseudomonas Cytochrome c Peroxidase. XI. Kinetics of the Peroxidatic Oxidation of Pseudomonas Respiratory Chain Components. Rönnberg, Marjaana; Ellfolk, Nils Pages: 719-727. DOI number: 10.3891/acta.chem.scand.29b-0719 |
Articles in volume 31b (1977)
The Amino Acid Sequence of Soybean (Glycine max) Leghemoglobin c. Sievers, Gunnel; Huhtala, Marja-Liisa; Ellfolk, Nils Pages: 723-724. DOI number: 10.3891/acta.chem.scand.31b-0723 |
Articles in volume 32b (1978)
The Primary Structure of Soybean (Glycine max) Leghemoglobin c. Sievers, Gunnel; Huhtala, Marja-Liisa; Ellfolk, Nils Pages: 380-386. DOI number: 10.3891/acta.chem.scand.32b-0380 |
Articles in volume 38b (1984)
The Formation of the Primary Hydrogen Peroxide Compound (Compound I) of Pseudomonas Cytochrome c Peroxidase as a Function of pH. Rönnberg, Marjaana; Ellfolk, Nils; Dunford, H. Brian Pages: 79-83. DOI number: 10.3891/acta.chem.scand.38b-0079 |
Articles in volume 17 supl. (1963)
Crystalline Leghemoglobin. VII. Magnetic and Spectrophotometric Properties of Leghemoglohin and its Derivatives. Ehrenberg, Anders; Ellfolk, Nils Pages: 343-347. DOI number: 10.3891/acta.chem.scand.17s-0343 |