Ebina S, Nagai Y
Clin Chem. 1979 Feb;25(2):247-51.
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.
通过对11种不同蛋白质（包括天然白蛋白和二硫键还原的白蛋白）用磺基水杨酸、2-萘磺酸、甲苯磺酸、二氯乙酸或三氯乙酸处理的研究，我们阐明了决定产生浊度的相互作用以及影响浊度的其他因素，并讨论了这种比浊法的临床实用性。在决定浊度方面，至少有三种相互作用很重要：蛋白质上正电荷的减少、未电离的氯乙酸与蛋白质的氢键形成以及芳香族磺酸与白蛋白的疏水相互作用。浊度会因酸和蛋白质的种类、酸的浓度、温度以及加酸后的静置时间而有明显变化。我们得出结论，这项技术应仅限于确认蛋白尿。
