The effect of surfactant structure on ribonuclease A–surfactant interactions
Copyright policy )The effect of surfactant structure on ribonuclease A–surfactant interactions
The enzymic activity of ribonuclease A was measured in the presence of several surfactants at pH7.2. Cationic surfactants with trimethylammonium and pyridinium head groups do not deactivate or denature the enzyme, whereas n-dodecylamine hydrochloride, like the anionic surfactant sodium n-dodecyl sulphate, deactivates and denatures ribonuclease A.
- University of Salford United Kingdom
Protein Denaturation, Nucleotides, Sodium Dodecyl Sulfate, Pyridinium Compounds, Cytidine, Hydrogen-Ion Concentration, Quaternary Ammonium Compounds, Kinetics, Structure-Activity Relationship, Surface-Active Agents, Ribonucleases, Spectrophotometry, Ultraviolet
Protein Denaturation, Nucleotides, Sodium Dodecyl Sulfate, Pyridinium Compounds, Cytidine, Hydrogen-Ion Concentration, Quaternary Ammonium Compounds, Kinetics, Structure-Activity Relationship, Surface-Active Agents, Ribonucleases, Spectrophotometry, Ultraviolet
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