The behaviors of Ca2+-ATPase embedded in interdigitated bilayer

被引:7
|
作者
Lu, JZ [1 ]
Huang, F [1 ]
Chen, JW [1 ]
机构
[1] Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源
JOURNAL OF BIOCHEMISTRY | 1999年 / 126卷 / 02期
关键词
Ca2+-ATPase; interdigitated bilayer; lysophosphatidylcholine;
D O I
10.1093/oxfordjournals.jbchem.a022449
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We investigated the behavior of a membrane protein, Ca2+-ATPase, in interdigitated phospholipid bilayers, The results showed that Ca2+-ATPase does not cause significant alterations in the interdigitation of 16:0 LPC/DPPC (27.0 mol% LPC) vesicles when it is reconstituted with lipids. Intrinsic fluorescence, acrylodan fluorescent adducts, and CD spectra indicated that Ca2+-ATPase, when embedded in interdigitated bilayer structures, is more exposed to the hydrophilic environment and has a looser structure than when embedded in non-interdigitated bilayers, The interdigitation of acyl chains induces a rapid loss of enzyme activity, It is suggested that interdigitated bilayer structures may play an important role as negative regulatory factors in physiological functions.
引用
收藏
页码:302 / 306
页数:5
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