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.
D003562:Cytidine / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009711:Nucleotides / Q000378:metabolism*; D011489:Protein Denaturation; D011726:Pyridinium Compounds; D000644:Quaternary Ammonium Compounds; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship; D013501:Surface-Active Agents / Q000378:metabolism* / Q000494:pharmacology
D009711:Nucleotides; D011726:Pyridinium Compounds; D000644:Quaternary Ammonium Compounds; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate; D003562:Cytidine; D012260:Ribonucleases