Maximov G V, Kols O R
Gen Physiol Biophys. 1985 Jun;4(3):279-85.
The mechanism of activation of Na, K-ATPase in nerve fibres during rhythmic excitation was studied. 3H-ouabain binding to the nerve was found to be dependent on the frequency of rhythmic excitation. During rhythmic excitation 3H-ouabain binding was increased in all nerves tested. The maximum of 3H-ouabain binding in squid and crab nerves was observed at 10 impulses/s, and in frog nerve at 100 impulses/s. The level of bound glycoside decreased during high-frequency excitation. Rhythmic excitation did not change Na, K-ATPase affinity to ouabain, but it appeared to increase the concentration of ouabain sensitive sites in the nerve membrane. The enhancement of 3H-ouabain binding to nerve during rhythmic excitation is interpreted as arising from transformation of "inactive" forms of the enzyme to "active" ones.
研究了神经纤维在节律性兴奋过程中钠钾ATP酶的激活机制。发现3H-哇巴因与神经的结合取决于节律性兴奋的频率。在节律性兴奋过程中,所有测试神经中3H-哇巴因的结合均增加。在鱿鱼和蟹神经中,3H-哇巴因结合的最大值在10次冲动/秒时观察到,而在蛙神经中在100次冲动/秒时观察到。在高频兴奋期间,结合糖苷的水平下降。节律性兴奋并未改变钠钾ATP酶对哇巴因的亲和力,但似乎增加了神经膜中哇巴因敏感位点的浓度。节律性兴奋期间3H-哇巴因与神经结合的增强被解释为是由于酶的“无活性”形式转变为“活性”形式所致。