Iwaata H, Baba A, Matsuda T
Jpn J Pharmacol. 1974 Dec;24(6):817-23. doi: 10.1254/jjp.24.817.
The properties of soluble and microsomal thiamine triphosphatase (TTPase) in rat brain were examined. The subcellular distributions and the pH optima of these enzyme activities differ markedly. TTPase seems to be distinct from a general nucleoside triphosphatase. The TTPase activities have an absolute divalent cation requirement which is fulfilled by Mg-++ or Ca-++ in microsomes and by Mg-++, but not Ca-++, in the soluble fraction. Addition of a physiological concentration of Ca-++ markedly inhibited the soluble TTPase activity.
对大鼠脑中可溶性和微粒体硫胺素三磷酸酶（TTPase）的特性进行了研究。这些酶活性的亚细胞分布和最适pH值有显著差异。TTPase似乎不同于一般的核苷三磷酸酶。TTPase活性绝对需要二价阳离子，微粒体中的活性由Mg++或Ca++满足，而可溶性部分中的活性仅由Mg++满足，Ca++不能满足。添加生理浓度的Ca++可显著抑制可溶性TTPase活性。
