Aseychev A V, Azizova O A, Beckman E M, Skotnikova O I, Piryazev A P, Dobretsov G E
Laboratory for Biophysical Bases of Pathology, Federal State Institution, Institute of Physicochemical Medicine, Federal Medical-Biological Agency, Moscow, Russia.
Bull Exp Biol Med. 2012 Aug;153(4):463-7. doi: 10.1007/s10517-012-1741-5.
The dynamics of albumin transport function was studied during metal-catalyzed oxidation of albumin in diluted blood plasma from healthy donors and in the solution of purified albumin using fluorescent probe K-35. The changes were compared with the dynamics of free radical oxidation markers. For oxidation, different concentrations of Cu(2+), Fe(2+), Fe(3+) ions as well as EDTA and H(2)O(2) were used. Oxidative modification of proteins was assessed by carbonyl and bityrosine fluorescent products. Oxidation of plasma lipids was assessed by the levels of TBA-reactive products. It was found that oxidation markedly decreased effective concentration of albumin characterizing albumin binding capacity, and leads to accumulation of carbonyl products of protein oxidation, bityrosine fluorescent products in proteins, and TBA-active products of lipid oxidation. It was hypothesized that reduced effective concentration of albumin is related to impairment of its binding sites and/or accumulation of free-radical oxidation products filling the binding sites of albumin.
利用荧光探针K-35，研究了健康供体稀释血浆中白蛋白在金属催化氧化过程中的转运功能动态变化，以及纯化白蛋白溶液中的相关情况。将这些变化与自由基氧化标志物的动态变化进行了比较。为进行氧化反应，使用了不同浓度的Cu(2+)、Fe(2+)、Fe(3+)离子以及EDTA和H(2)O(2)。通过羰基和双酪氨酸荧光产物评估蛋白质的氧化修饰。通过TBA反应性产物水平评估血浆脂质的氧化。研究发现，氧化显著降低了表征白蛋白结合能力的有效浓度，并导致蛋白质氧化的羰基产物、蛋白质中的双酪氨酸荧光产物以及脂质氧化的TBA活性产物积累。据推测，白蛋白有效浓度降低与其结合位点受损和/或填充白蛋白结合位点的自由基氧化产物积累有关。
