Leynadier D, Peyrot V, Codaccioni F, Briand C
Laboratoire de Physique Pharmaceutique, Faculté de Pharmacie, Marseille, France.
Chem Biol Interact. 1991;79(1):91-102. doi: 10.1016/0009-2797(91)90055-c.
We have studied the interaction of Na2SeO3 with microtubule proteins and tubulin. This selenium compound inhibits the polymerization of MTP (half-inhibition occurred for Na2SeO3 10 microM), and to a lesser that of tubulin. This effect of selenite is related to the formation of disulfide bridges between tubulin sulfhydryl groups, inducing a conformational change of the protein. This is corroborated by the modified binding of colchicine and vinblastine in presence of selenium. The selenite inhibitory concentrations are similar to the toxic blood levels of selenium (40 microM).
我们研究了亚硒酸钠与微管蛋白和微管蛋白的相互作用。这种硒化合物抑制微管蛋白（MTP）的聚合（10微摩尔的亚硒酸钠产生半数抑制），对微管蛋白的抑制作用较小。亚硒酸盐的这种作用与微管蛋白巯基之间二硫键的形成有关，从而诱导蛋白质的构象变化。在硒存在的情况下，秋水仙碱和长春花碱结合的改变证实了这一点。亚硒酸盐的抑制浓度与硒的毒性血液水平（40微摩尔）相似。
