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(钠+钾)-ATP酶的相对温度依赖性

Comparative temperature dependence of (Na+ + K+)-ATPase.

作者信息

Russell J C, Chambers M M

出版信息

Physiol Chem Phys. 1976;8(3):237-51.

PMID:138144
Abstract

The temperature dependence of (Na+ + K+)-ATPase was measured, utilizing preparations of enzyme from heat and kidney of rats, hamsters, guinea pigs, ground squirrels, turtles, chickens, and ducks. The two hibernating species, hamsters and ground squirrels, were studied awake at normothermia and hibernating at 4 degrees C. The results for every species except the turtles showed the same temperature dependence established for (Na++K+)-ATPase from rabbit kidney with a quasi-linear dependence above 15 degrees C and little or no activity below 15 degrees C. Turtle enzymes showed a broad activity versus temperature curve with a fall-off at high and low temperatures. The data in all cases, including the turtle data, may be fitted by a previously described thermodynamic kinetic model. Further, the model will fith the turnover or decrease in enzyme activity at higher temperatures observed in a number of cases. These results do not support the widely imputed ion pumping role for (Na++K+)-ATPase.

摘要

利用大鼠、仓鼠、豚鼠、地松鼠、龟、鸡和鸭的心脏和肾脏的酶制剂,测量了(Na + + K +)-ATP酶的温度依赖性。研究了两种冬眠动物,仓鼠和地松鼠,分别在正常体温下清醒状态以及在4摄氏度冬眠状态下进行研究。除龟以外的每个物种的结果显示,(Na + + K +)-ATP酶与兔肾中的(Na + + K +)-ATP酶具有相同的温度依赖性,在15摄氏度以上呈准线性依赖,在15摄氏度以下几乎没有活性。龟的酶显示出较宽的活性与温度曲线,在高温和低温下活性均下降。所有情况下的数据,包括龟的数据,都可以用先前描述的热力学动力学模型进行拟合。此外,该模型将适用于在许多情况下观察到的较高温度下酶活性的周转或降低。这些结果不支持广泛认为的(Na + + K +)-ATP酶的离子泵作用。

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