Pecci L, Pensa B, Costa M, Cignini P L, Cannella C
Biochim Biophys Acta. 1976 Aug 12;445(1):104-11. doi: 10.1016/0005-2744(76)90163-7.
The reaction between bovine rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) and reduced dithiothreitol has been studied. This reagent, in the absence of thiosulfate, reduces the amount of sulfur carried by rhodanese with formation of sulfide and oxidized dithiothreitol: E-S-SH + reduced dithiothreitol replaced by E-SH + HS- + oxidized dithiothreitol, (E = enzyme). An inactivation was observed at high dithiothreitol/enzyme ratios or at very low enzyme concentrations. The inactivation was not observed in the presence of thiosulfate and can be reversed by cyanide or thiosulfate. A thiosulfate reduction activity of rhodanese was also found using dithiothreitol as reductant.
对牛硫氰酸酶（硫代硫酸盐：氰化物硫转移酶，EC 2.8.1.1）与还原型二硫苏糖醇之间的反应进行了研究。在没有硫代硫酸盐的情况下，该试剂会减少硫氰酸酶携带的硫量，形成硫化物和氧化型二硫苏糖醇：E-S-SH + 还原型二硫苏糖醇 被 E-SH + HS- + 氧化型二硫苏糖醇取代，（E = 酶）。在高二硫苏糖醇/酶比例或极低酶浓度下观察到失活现象。在硫代硫酸盐存在的情况下未观察到失活现象，并且可以通过氰化物或硫代硫酸盐逆转。还发现以二硫苏糖醇作为还原剂时，硫氰酸酶具有硫代硫酸盐还原活性。
