首页> 外文OA文献 >Saturation transfer EPR measurements of the rotational motion of a strongly immobilized ouabain spin label on renal Na, K-ATPase11The Na,K-ATPase preparations used here consisted of membrane fragments containing the ATPase.

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Saturation transfer EPR measurements of the rotational motion of a strongly immobilized ouabain spin label on renal Na, K-ATPase11The Na,K-ATPase preparations used here consisted of membrane fragments containing the ATPase.

机译：饱和固定的哇巴因自旋标记物在肾Na，K-ATPase11上的旋转运动的饱和转移EPR测量此处使用的Na，K-ATPase制剂由含有ATPase的膜片段组成。

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Mahaney James E.; Girard Jaymee P.; Grisham Charles M.;
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1. Saturation transfer EPR measurements of the rotational motion of a strongly immobilized ouabain spin label on renal Na, K‐ATPase [J] . Girard Jaymee P., Grisham Charles M., Mahaney James E. FEBS Letters . 1990,第2期

机译：饱和固定的哇巴因自旋标记物在肾Na，K-ATPase上的旋转运动的饱和转移EPR测量
2. Microsecond motions of the lipids associated with trypsinized Na,K-ATPase membranes. Progressive saturation spin-label electron spin resonance studies. [J] . Arora A, Esmann M, Marsh D Biochemistry . 1999,第31期

机译：与胰蛋白酶消化的Na，K-ATPase膜相关的脂质的微秒运动。逐步饱和自旋标记电子自旋共振研究。
3. Membrane fluidity profiles as deduced by saturation-recovery EPR measurements of spin-lattice relaxation times of spin labels [J] . Mainali L., Feix J.B., Hyde J.S., Journal of magnetic resonance . 2011,第2期

机译：通过自旋标记的自旋晶格弛豫时间的饱和度恢复EPR测量得出的膜流动性曲线
4. Membrane fluidity profiles as deduced by saturation-recovery EPR measurements of spin-lattice relaxation times of spin labels [O] . Laxman Mainali, Jimmy B. Feix, James S. Hyde, -1

机译：通过饱和恢复EPR测量旋转标签的旋转晶格弛豫时间推出的膜流动性曲线
5. Membrane Fluidity Profiles as Deduced by Saturation-Recovery EPR Measurements of Spin-Lattice Relaxation Times of Spin Labels: Multifrequency Approach [O] . Mainali Laxman, Hyde James S., Subczynski Witold K. 2012

机译：通过自旋标签的自旋晶格弛豫时间的饱和恢复EPR测量得出的膜流动性曲线：多频方法

Saturation transfer EPR measurements of the rotational motion of a strongly immobilized ouabain spin label on renal Na, K-ATPase11The Na,K-ATPase preparations used here consisted of membrane fragments containing the ATPase.

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