Bulk properties of the lipid bilayer are not essential for the thermal stability of Na,K-ATPase from shark rectal gland or pig kidney.
Bulk properties of the lipid bilayer are not essential for the thermal stability of Na,K-ATPase from shark rectal gland or pig kidney.
复制标题
脂质双层的整体特性对于来自鲨鱼直肠腺或猪肾的 Na,K-ATP 酶的热稳定性并不重要。
DOI：
10.1016/j.bbrc.2011.02.094
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发表时间：
2011
影响因子：
3.1
通讯作者：
M. Esmann
中科院分区：
文献类型：
--
作者：
A. S. Hansen;Kristian L Kraglund;N. Fedosova;M. Esmann
猪肾Na，K-ATPase的热稳定性明显高于鲨鱼盐腺Na，K-ATPase。的脂质双层的作用进行了研究，通过溶解的膜结合的酶在非离子洗涤剂八甘醇十二烷基单醚（C12 E8），添加过量的二油酰磷脂酰胆碱（DOPC）或棕榈油酰磷脂酰胆碱（POPC）和重建的膜通过去除洗涤剂。在54°C下，重构的具有酶活性的猪酶保持高的热稳定性，并且重构的鲨鱼酶保持低的热稳定性，即使具有9倍过量的DOPC。该结果表明，热稳定性差异的起源与天然膜的整体脂质性质无关。
The thermal stability of Na,K-ATPase from pig kidney is markedly greater than that of Na,K-ATPase from shark salt glands. The role of the lipid bilayer is studied by solubilisation of the membrane-bound enzyme in the nonionic detergent octaethyleneglycoldodecylmonoether (C12E8), addition of excess dioleylphosphatidylcholine (DOPC) or palmitoyloleylphosphatidylcholine (POPC) and reconstitution of membranes by removal of detergent. At 54°C the reconstituted enzymatically active pig enzyme retains a high thermal stability, and reconstituted shark enzyme retains a low thermal stability, even with a 9-fold excess of DOPC. This result suggests that the origin of the difference in thermal stability is not related to bulk lipid properties of the native membranes.