Re-evaluation of turbidimetry of proteins by use of aromatic sulfonic acids and chloroacetic acids.
From studies on 11 different proteins (including native albumin and albumin with reduced disulfide-bridges) treated with sulfosalicylic, 2-naphthalenesulfonic, toluenesulfonic, dichloroacetic, or trichloroacetic acids, we elucidate the interactions determining the resulting turbidities and other factors affecting turbidities, and we discuss the clinical utility of such turbidimetry. At least three interactions are important in determining turbidity: reduction of positive charges on the protein, hydrogen bonding of the non-ionized chloroacetic acids with the protein, and hydrophobic interaction of the aromatic sulfonic acids with albumin. Turbidity varies appreciably with the species of acid and protein, concentrations of acid, temperature, and standing time after acid is added. We conclude that this technique should be restricted to confirming proteinuria.
D000418:Albumins; D001190:Arylsulfonates; D003999:Dichloroacetic Acid; D006860:Hydrogen Bonding; D007782:Lactoglobulins; D009391:Nephelometry and Turbidimetry; D010084:Oxidation-Reduction; D010783:Photometry; D011506:Proteins / Q000032:analysis*; D012459:Salicylates; D014238:Trichloroacetic Acid
D000418:Albumins; D001190:Arylsulfonates; D007782:Lactoglobulins; D011506:Proteins; D012459:Salicylates; D014238:Trichloroacetic Acid; D003999:Dichloroacetic Acid