Makarchikov A F, Chernikevich I P
Laboratory of Applied Enzymology and Biotechnology, Academy of Sciences of Belarus, Grodno.
Biochem Mol Biol Int. 1998 Sep;46(1):115-23. doi: 10.1080/15216549800203622.
Properties of soluble thiamine triphosphatase (ThTPase), adenosine triphosphatase, nucleoside triphosphatase and alkaline phosphatase activities in bovine kidney were compared. ThTPase and the other phosphatases differed clearly in their pH-dependences, K(m) and molecular masses. Apparent K(m) and pH optimum for ThTPase were determined to be 45.5 microM and 8.9, respectively. Molecular mass of the enzyme was 29.1 kDa as estimated by Sephadex G-100 gel filtration. The results obtained show bovine kidney to contain a specific soluble ThTPase, this enzyme being the only one hydrolyzing low concentrations of ThTP.
比较了牛肾中可溶性硫胺素三磷酸酶（ThTPase）、腺苷三磷酸酶、核苷三磷酸酶和碱性磷酸酶活性的特性。ThTPase与其他磷酸酶在pH依赖性、米氏常数（K(m)）和分子量方面存在明显差异。ThTPase的表观K(m)和最适pH分别测定为45.5微摩尔和8.9。通过Sephadex G - 100凝胶过滤估计该酶的分子量为29.1 kDa。所得结果表明牛肾中含有一种特异性可溶性ThTPase，该酶是唯一能水解低浓度ThTP的酶。
