Eftink M R, Ghiron C A
Department of Chemistry, University of Mississippi, University 38677.
Biochim Biophys Acta. 1987 Dec 18;916(3):343-9. doi: 10.1016/0167-4838(87)90179-8.
We have studied the protein concentration dependence of the acrylamide quenching of the fluorescence of the proteins, human serum albumin and monellin, and we have found no such dependence for the concentration range of 0.5-20 mg/ml. These quenching studies were performed by fluorescence lifetime measurements using phase/modulation fluorometry. We have also performed equilibrium dialysis studies, which show no large degree of association of acrylamide with serum albumin, and we have found that acrylamide has only a small effect on the activity of selected enzymes. These various studies do not indicate the existence of strong acrylamide-protein interactions and are in discord with a recent report by Blatt et al. in this journal (Blatt, E., Husain, A. and Sawyer, W.H. (1986) Biochim. Biophys. Acta 871, 6-13).
我们研究了丙烯酰胺对蛋白质（人血清白蛋白和莫内林）荧光淬灭的蛋白质浓度依赖性，发现在0.5 - 20 mg/ml的浓度范围内不存在这种依赖性。这些淬灭研究是通过使用相位/调制荧光法进行荧光寿命测量来完成的。我们还进行了平衡透析研究，结果表明丙烯酰胺与血清白蛋白没有高度的结合，并且我们发现丙烯酰胺对所选酶的活性只有很小的影响。这些不同的研究并未表明存在强烈的丙烯酰胺 - 蛋白质相互作用，这与布拉特等人在本期刊上最近发表的一篇报告（布拉特，E.，侯赛因，A.和索耶，W.H.（1986年）《生物化学与生物物理学报》871卷，6 - 13页）不一致。
