Sogami M, Inouye H, Nagaoka S, Era S
Int J Pept Protein Res. 1982 Sep;20(3):254-8. doi: 10.1111/j.1399-3011.1982.tb03055.x.
By working at very low protein concentration (ca. 0.003%), it is possible to measure tryptophyl fluorescence intensity at 350 nm (F350) of bovine plasma albumin (BPA) as a function of pH under precipitating conditions (acidic concentrated salt solutions). Under such conditions, distinct changes in F350 were seen before the starting of precipitation of BPA and no further changes in F350 over the precipitating pH range. Comparison of pH-profiles monitored by F350 with those by solubility in the presence of various salts at various concentrations indicated that the change of solubility is observed after definite changes in conformation of the protein.
通过在极低蛋白质浓度（约0.003%）下进行实验，可以在沉淀条件（酸性浓盐溶液）下测量牛血浆白蛋白（BPA）在350 nm处的色氨酸荧光强度（F350）随pH的变化。在这种条件下，在BPA开始沉淀之前F350有明显变化，而在沉淀的pH范围内F350没有进一步变化。将F350监测的pH曲线与不同浓度各种盐存在下的溶解度曲线进行比较表明，在蛋白质构象发生一定变化后才观察到溶解度的变化。
