Organization of Lipids in Sarcoplasmic Reticulum Membrane and Ca2+-dependent ATPase Activity

The organization of lipids in sarcoplasmic reticulum membrane was studied with a variety of stearic spin labels and a phosphatidylcholine spin label. The ESR spectra of the spin-labeled membranes consisted of two components, one due to labels in lipid bilayer structure and the other due to more immo...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1975-11, Vol.78 (5), p.1039-1045
Main Authors: NAKAMURA, Machiko, OHNISHI, Shun-ichi
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - analysis
Calcium - pharmacology
Electron Spin Resonance Spectroscopy
Membranes - analysis
Phospholipases
Phospholipids - analysis
Sarcoplasmic Reticulum - analysis
Spin Labels
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Summary:The organization of lipids in sarcoplasmic reticulum membrane was studied with a variety of stearic spin labels and a phosphatidylcholine spin label. The ESR spectra of the spin-labeled membranes consisted of two components, one due to labels in lipid bilayer structure and the other due to more immobilized labels. The relative intensity of the immobilized component increased when the lipid content of the membrane was decreased by treatment with phospholipase A [EC 3. 1. 1. 4] and subsequent washing with bovine serum albumin. Membrane containing 30% of the intact phospholipid, i.e. 0.15 mg of phospholipid per mg of protein, showed a spectrum consisting only of the immobilized component (the overall splitting ranged from 58.5 G to 60.5 G). The immobilized component was ascribed to lipids complexed with protein. The fraction of lipids in the two different organizations was determined from the ESR spectrum. The activity of the Ca2+-Mg2+ dependent ATPase (ATP phosphohydrolase, EC 3. 6. 1. 3] was found to increase almost linearly with the lipid bilayer content in the membrane, whereas phosphoenzyme formation was almost independent of the bilayer content. This indicates that the bilayer structure is necessary for the ATPase to attain its full transport activity.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a130981