Protein-Ionic Detergent Interaction

摘要: Abstract The volume effects produced by the reaction of sodium dodecyl sulfate with bovine serum albumin were determined dilatometrically at 30.0 ± 0.001°. calculated isotherms indicate operation least two major processes: (a) a decrease which is caused high affinity protein-detergent interaction and occurs detergent concentrations ranging from 0.02 to 0.08 m; (b) increase SDS g0.08 m attributed structurally altered protein. At less than either positive or negative changes are depending on type ionic charge effect pH was investigated comparing 5.1 8; negatively charged exhibited more pronounced compared isoionic albumin. unique function composition, structural organization, Acrylamide gel electrophoretic studies these systems reveal generation categories complexes. low ratios (SDS) protein, there progressive mobility protein complexes increasing anion concentration. concentration ≥0.02 another component formed whose substantially faster that observed lower concentrations. ≥0.08 this only present; invariant in region 0.5 SDS.