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- W47296823 abstract "ABSTRACT Sarcoplasmic reticulum vesicles derived from rabbit skeletal muscle consist mainly of the intrinsic membrane Ca 2+ pump protein, two membrane associated proteins, and phospholipid. Vesicles dissociated using deoxycholate were reassembled by dialysis with restoration of energized Ca 2+ accumulation capacity. The solubilized Ca 2+ pump protein binds about 1/3 of the phospholipid present in the native membrane and is present in a low aggregation state. During the initial stages of membrane assembly after partial removal of detergent by dialysis, Ca 2+ pump protein aggregates are formed which bind non-specifically amounts of phospholipid similar to those in the solubilized protein. As membrane assembly proceeds, increasing amounts of phospholipid are rebound resulting in the formation of enclosed vesicles which trap 3 H-inulin and can support accumulation of Ca 2+ in the presence of ATP. The Ca 2+ pump protein in reconstituted vesicles appears to have lost its characteristic asymmetric arrangement within the hydrophobic center of the membrane, as indicated by freeze-fracture studies. About 70 – 90% of the Ca 2+ pump protein in the reassembled membrane is accessible to rapid trypsin digestion as opposed to 100% in the native membrane, suggesting that the protein may be also differently arranged at the membrane surface. Reconstituted vesicles pump Ca 2+ with a lower efficiency than native vesicles, possibly due to the different orientation of the Ca 2+ pump protein and/or the presence of vesicles which have not reformed a full permeability barrier for Ca 2+ ." @default.
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- W47296823 date "1978-01-01" @default.
- W47296823 modified "2023-10-18" @default.
- W47296823 title "REASSEMBLY OF SARCOPLASMIC RETICULUM MEMBRANE" @default.
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- W47296823 doi "https://doi.org/10.1016/b978-0-08-022626-2.50019-5" @default.
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