The behaviors of Ca(2+)-ATPase embedded in interdigitated bilayer

We investigated the behavior of a membrane protein, Ca(2+)-ATPase, in interdigitated phospholipid bilayers. The results showed that Ca(2+)-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 fl...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1999-08, Vol.126 (2), p.302-306
Main Authors: Lu, J Z, Huang, F, Chen, J W
Format: Article
Language:English
Subjects:
1,2-Dipalmitoylphosphatidylcholine - chemistry
Animals
Calcium-Transporting ATPases - metabolism
Circular Dichroism
Fluorescence Polarization
Lipid Bilayers - metabolism
Proteolipids - metabolism
Rabbits
Sarcoplasmic Reticulum - enzymology
Spectrometry, Fluorescence
Temperature
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Summary:We investigated the behavior of a membrane protein, Ca(2+)-ATPase, in interdigitated phospholipid bilayers. The results showed that Ca(2+)-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 Ca(2+)-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.
ISSN:0021-924X