[Inactivation of yeast inorganic pyrophosphatase by sodium dodecyl sulfate and cetyltrimethyl ammonium bromide].
The kinetics of the inactivation of yeast inorganic pyrophosphatase by sodium dodecyl sulfate (SDS) and cetyltrimethyl ammonium bromide were studied. Micellar forms of detergents were shown to be an active reagetns under conditions tudied. The possible scheme of the inactivation including reversible formation of the micellar-protein complex and subsequent penetration of the bound detergent molecules in the protein is proposed. The enzyme ionogenic group with pK 7-8 by 25 degrees C is found to be responsible for conformational changes of the enzymes. The influence of the specific ligands on inactivation of yeast pyrophosphatase by SDS is studied, and dissociations constants of corresponding enzyme-ligand complexes are calculated.
D002593:Cetrimonium Compounds / Q000494:pharmacology*; D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors*; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*
D002593:Cetrimonium Compounds; D008024:Ligands; D000644:Quaternary Ammonium Compounds; D012967:Sodium Dodecyl Sulfate; D011755:Pyrophosphatases
Inaktivatsiia neorganicheskoi pirofosofatazy is drozhzhei dodetsilsul' fatom natririia i bromistym tsetiltrimetilammoniem