兔腰大肌和鸡胸大肌三聚磷酸酶特性的比较研究

Comparative study on Tripolyphosphatase properties of rabbit psoas major and chicken pectoralis major

分离纯化兔腰大肌和鸡胸大肌中的三聚磷酸盐酶（TPPase），比较不同物种TTPase的酶学特性和作用条件。试验结果，显示兔腰大肌和鸡胸大肌的TPPase的最适温度分别为35℃和30℃；最适pH分别是6和5。Mg^2＋对兔腰大肌和鸡胸大肌的TPPase都有激活作用，在0～20mmol／L范围内，鸡胸大肌TPPase活性随Mg^2＋浓度增加而缓慢上升，3mmol／L的Mg^2＋对兔腰大肌TPPase激活作用最明显。Ca^2＋对兔腰大肌TPPase有激活作用，而对鸡胸大肌TPPase有抑制作用。高浓度的EDTA—Na4和KIO3对两种肉TPPase都有明显的抑制效果。EDTA—Na2对兔腰大肌TPPase的活性没有显著影响，但在高于0．5mmol／L时，对鸡胸大肌TPPase的活性抑制效果明显。

Properties of Tripolyphosphatase extracted and purified from rabbit psoas major and chicken pectoralis major were studied to compare the difference and reactive conditions between different species in enzymatic properties. The optimum temperatures of rabbit psoas major and chicken peetoralis major muscle were 35 ℃ and 30 ℃, respectively. The optimum pH was 6 and 5, respectively. TPPase activity was activated by Mg^2＋ with maximum activation at 3 mmol/L of rabbit psoas major, TPPase activity of chicken pectoralis major slowly increased with Mg^2＋ concentration. Ca^2＋ enhanced TPPase activity of rabbit psoas major and showed adverse effect on that of chicken pectoralis major. TPPase activity of rabbit psoas major and chicken peetoralis major was inhibited by EDTA-Na4 and KIO3 at high concentration. E TA-Na2 had no effects on TPPase activity of rabbit psoas majormajor, however, it did inhibit the enzyme activity consumingly in more than 0. 5 mmol/L.