Voskoboyev A I, Averin V A
Acta Vitaminol Enzymol. 1983;5(4):251-4.
A protein with thiamine-binding activity (14 nmole/mg protein) was isolated from rat red cells by affinity chromatography. Adsorbent with varying degrees of hydrophobicity containing thiamine as ligand were used for the isolation. A 2300-fold purification in a 50% overall yield was attained. The purified thiamine-binding protein is homogeneous on polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate.
通过亲和层析从大鼠红细胞中分离出一种具有硫胺素结合活性的蛋白质(14 纳摩尔/毫克蛋白质)。使用含有硫胺素作为配体的不同程度疏水性的吸附剂进行分离。实现了 2300 倍的纯化,总产率为 50%。在十二烷基硫酸钠存在下,纯化的硫胺素结合蛋白在聚丙烯酰胺凝胶电泳上呈现均一性。