Interaction of muscle pyruvate kinase with 1,8-anilinonaphthalene sulfonate
| Autor: | Clarence H. Suelter, K.C. Ingham |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Pyruvate dehydrogenase kinase
Chemical Phenomena Macromolecular Substances Stereochemistry Phenylalanine Pyruvate Kinase Biophysics Biology Biochemistry Anilino Naphthalenesulfonates Phosphoenolpyruvate chemistry.chemical_compound Animals Magnesium Molecular Biology chemistry.chemical_classification Muscles Osmolar Concentration Fluorescence Adenosine Diphosphate Enzyme Activation Dissociation constant Chemistry Kinetics Spectrometry Fluorescence Enzyme Sulfonate chemistry Potassium Rabbits Phosphoenolpyruvate carboxykinase Mathematics Pyruvate kinase Protein Binding |
| Zdroj: | Archives of Biochemistry and Biophysics. 168:531-535 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(75)90284-2 |
| Popis: | The interaction of the fluorescent probe 1,8-anilinonaphthalene sulfonate with rabbit muscle pyruvate kinase is reported. Four moles of 1,8-anilinonaphthalene sulfonate interact per mole of the 4-subunit enzyme with a dissociation constant of 1.7 × 10−4 m at 30 °. The interaction is not competitive with substrates ADP and phosphoenolpyruvate, with cations K+ and Mg2+, nor with effector phenylalanine. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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