Ouabain sensitivity of the alpha 3 isozyme of rat Na,K-ATPase.
Ouabain sensitivity of the alpha 3 isozyme of rat Na,K-ATPase.
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大鼠 Na,K-ATP 酶的 α3 同工酶哇巴因敏感性。
DOI：
10.1016/s0006-291x(88)80914-8
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发表时间：
1988
影响因子：
3.1
通讯作者：
Sweadner,KJ
中科院分区：
文献类型：
--
作者：
Urayama,O;Sweadner,KJ
大鼠脑干轴膜Na，K-ATP酶含有其催化亚基的两种同工酶α 2和α 3。为了从功能上分离α 3同工酶，用胰蛋白酶处理纯化的轴膜Na，K-ATPase。使用同工酶特异性抗体对胰蛋白酶处理的Na，K-ATP酶进行免疫印迹分析表明，α 3比α 2对消化的抵抗力更强。胰蛋白酶抗性α 3同工酶组分（不含α 2）含有50-60%的ATP酶活性，在0.13 μM时被哇巴因抑制一半。这表明α 3 Na，K-ATP酶同工酶对强心苷类物质具有较高的敏感性。
The Na,K-ATPase of rat brainstem axolemma membranes contains two isozymes of its catalytic subunit, alpha 2 and alpha 3. To isolate the alpha 3 isozyme functionally, purified axolemma Na,K-ATPase was treated with trypsin. Immunoblot analysis of trypsin-treated Na,K-ATPase using isozymespecific antibodies showed that alpha 3 was significantly more resistant to digestion than alpha 2. The trypsin-resistant alpha 3 isozyme fraction, devoid of alpha 2, contained 50–60% of the ATPase activity, and was inhibited by ouabain half-maximally at 0.13 μM. This indicates that the alpha 3 Na,K-ATPase isozyme has a high sensitivity to cardiac glycosides.