Abstract
The (Ca2+-Mg2+)-ATPase from sarcoplasmic reticulum has been reconstituted into phospholipid bilayers of different fatty acyl chain length and degree of unsaturation, and ATPase activity was found to vary about 10-fold. Order parameters for bilayers of these lipids measured using the ESR probe 5-doxylstearic acid varied from 0.5 to 0.6 at 37 degrees C. There was no correlation between phospholipid order parameter and ATPase activity, and we conclude that phospholipid structure is a more important determinant of protein activity than is membrane fluidity.
Original language | English |
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Pages (from-to) | 8070-1 |
Number of pages | 2 |
Journal | Journal of Biological Chemistry |
Volume | 259 |
Issue number | 13 |
Publication status | Published - 1984 |