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- W1604248953 abstract "Abstract The reconstitution of functional sarcoplasmic reticulum vesicles has been achieved. Sarcoplasmic reticulum vesicles at a concentration of 7.0 mg of protein per ml are solubilized with the use of 3.4 mg per ml of deoxycholate. The solubilized sample is nonmembranous as viewed in the electron microscope. Sedimentation studies indicate it is dissociated largely into protein and phospholipid. Removal of the detergent by dialysis results in the reaggregation of protein and phospholipid to form membranous vesicles which are capable of energized Ca2+ accumulation. The reconstitution is temperature dependent being optimal at about 20°; function is not restored if dialysis is carried out at 0–4°. The composition of the dialysis buffer which favors reconstitution is 0.4 m KCI, 1.5 mm Mg2+-1.0 mm ethylenediaminetetraacetate, and 0.1 mm Ca2+, pH 7.25. Reconstituted and original sarcoplasmic reticulum vesicles have a similar phospholipid content and buoyant density. The Ca2+ pump protein is the major protein in both reconstituted and original vesicles; however, the two other major proteins with a molecular weight of approximately 55,000 are only in part rebound. The reconstituted vesicles have an elevated adenosine triphosphatase activity. Energized Ca2+ uptake capacities measured in the presence and absence of oxalate are restored to about 50% and 25%, respectively." @default.
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- W1604248953 date "1974-01-01" @default.
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- W1604248953 title "Dissociation and Reconstitution of Functional Sarcoplasmic Reticulum Vesicles" @default.
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- W1604248953 doi "https://doi.org/10.1016/s0021-9258(19)43125-6" @default.
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