Protein-cationic detergent interaction. Interaction of bovine serum albumin and other proteins with alkylpyridinium bromides studied by viscosity, gel filtration and spin-label methods.
Viscosity, gel filtration and spin-labelling methods have been used to study the influence of alkylpyridinium bromides on the conformation of bovine serum albumin and other proteins. Cationic detergents cause partial unfolding of the native protein molecules. The magnitude of these changes increases with increasing length of the detergent hydrocarbon chain. When cationic detergents are added to reduced and carboxymethylated bovine serum albumin the observed changes are opposite to those found in native protein.
D000818:Animals; D002412:Cations; D002417:Cattle; D002850:Chromatography, Gel; D003902:Detergents; D004578:Electron Spin Resonance Spectroscopy; D007700:Kinetics; D011487:Protein Conformation / Q000187:drug effects; D011506:Proteins; D011726:Pyridinium Compounds; D012710:Serum Albumin, Bovine; D013329:Structure-Activity Relationship; D014783:Viscosity
D002412:Cations; D003902:Detergents; D011506:Proteins; D011726:Pyridinium Compounds; D012710:Serum Albumin, Bovine