[肾脏钠钾ATP酶的热失活动力学]
[Kinetics of thermoinactivation of kidney Na+-,K+-ATPase].
作者信息
Kravtsova V V, Kravtsov A V, Kaplia A A, Gorishniak V P
出版信息
Ukr Biokhim Zh (1978). 1985 Nov-Dec;57(6):23-8.
The studies of Na+,K+-ATPase (the fraction of microsomes and highly active preparation) thermoinactivation in kidneys at 50, 55 and 60 degrees C under conditions of the different ionic composition of the medium has shown that 20 mM K+ protects the enzymic complex from the thermal denaturation more effectively than 182 mM Na+ does. An increase in the Mg2+ concentration in the medium from 1 to 5 mM decreases Na+,K+-ATPase resistance to thermoinactivation. The enzyme half-life becomes almost thrice as low in this case. The results obtained are discussed from the standpoint of specificity of ion-induced conformational states of Na+,K+-ATPase and regulatory role of cations in the process of its functioning.
在不同离子组成的介质条件下，对肾脏中Na⁺,K⁺-ATP酶（微粒体部分和高活性制剂）在50、55和60摄氏度下的热失活研究表明，20 mM K⁺ 比182 mM Na⁺ 更有效地保护酶复合物免受热变性。介质中Mg²⁺ 浓度从1 mM增加到5 mM会降低Na⁺,K⁺-ATP酶对热失活的抗性。在这种情况下，酶的半衰期几乎降低为原来的三分之一。从Na⁺,K⁺-ATP酶离子诱导构象状态的特异性以及阳离子在其功能过程中的调节作用的角度对所得结果进行了讨论。
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