In protein analysis, fast techniques applicable for preliminary tests of the protein structural changes are sought. We show that using constant current chronopotentiometric stripping peak H, small amounts of oligomeric, denatured and aggregated bovine serum albumin (BSA) can be easily distinguished from native form. Different behavior of native, denatured, and aggregated BSA could be explained by combination of their different adsorption at charged surface and accessibility of electroactive amino acid residues. Ability to discriminate between individual forms allows to use chronopotentiometric stripping for study of processes responsible for structural changes, such as freezing treatment.

在蛋白质分析中，寻求适用于蛋白质结构变化初步测试的快速技术。我们表明，使用恒流计时电位剥离峰 H，可以很容易地将少量寡聚、变性和聚集的牛血清白蛋白 (BSA) 与天然形式区分开来。天然、变性和聚集 BSA 的不同行为可以通过它们在带电表面的不同吸附和电活性氨基酸残基的可及性来解释。区分个体形式的能力允许使用计时电位剥离来研究导致结构变化的过程，例如冷冻处理。