Abstract: A method and kit for precipitating protein from an aqueous solution consists of a quaternary ammonium cationic surfactant and a chaotropic salt, used in combination to reversibly precipitate proteins from the aqueous solution. Precipitation separates proteins that are entrapped, non-specifically, in the quaternary ammonium cationic surfactant:chaotropic salt complex as a pellet. The precipitated protein pellet is purified further by washing with an organic solvent to remove the surfactant:chaotrope complex, leaving behind pure, concentrated proteins that can be washed to purify further the protein and/or re-dissolved in whatever buffer is most suited for any successive procedure, such as analysis.

Abstract: An “in-gel” staining technique for detecting and/or separating proteins during electrophoresis, illustratively as a modification of the standard Laemmli procedure. A fluorescent dye, such as Nile red or Phosphine, is included in the running buffer (mobile phase) which may be a standard Laemmli Tris-Glycine SDS buffer that has been modified to reduce the concentration of detergent (SDS) to less than the typical concentration (0.10% v/v). The fluorescent dye stains proteins during electrophoretic separation. The post-electrophoretic operations are, therefor, reduced and the separated, stained fractions are recoverable for further processing, purifying or analysis.

Abstract: A process for preparing a bound antioxidant polymer concentrate is described which comprises grafting one or more acrylic or alkylacrylic esters or amides containing a hindered-amine group onto the polymer in the presence of a radical generator at a temperature of 100.degree. to 350.degree. C., the molar ratio of said radical generator to said ester or amide being from 0.001: to 1:1, the reaction being continued for a time such that the melt viscosity of the polymer which increases initially during the reaction has reduced to a level which permits the concentrate to be homogeneously blended subsequently into a unstabilized polymer.