Voskoboev A I, Artsukevich I M, Sotrovskiĭ Iu M
Biokhimiia. 1976 Dec;41(12):2196-200.
Using electrophoresis in polyacrylamide gel in the presence of sodium dodecyl sulfate thiamine pyrophosphokinase (EC 2.7.6.2) was found to possess quaternary structure and consist of two polypeptide chains. It was shown that besides active centres, the oligomer has allosteric centres for binding of Mg2+ ions, since treatment by HgCl2 and heating of the enzyme lead to complete "desensibilisation". This results in a disappearance of the S-shaped curve of the dependence of reaction rate on Mg2+ concentration, the Hill coefficient coming down to 1. It is assumed that thiamine pyrophosphokinase belongs to the class dissociating regulatory enzymes.
在十二烷基硫酸钠存在的情况下，利用聚丙烯酰胺凝胶电泳发现硫胺素焦磷酸激酶（EC 2.7.6.2）具有四级结构，由两条多肽链组成。结果表明，除活性中心外，该寡聚体还有结合Mg2+离子的别构中心，因为用HgCl2处理和加热该酶会导致完全“脱敏”。这导致反应速率对Mg2+浓度依赖性的S形曲线消失，希尔系数降至1。据推测，硫胺素焦磷酸激酶属于解离调节酶类。
