Temperature dependence of ATP hydrolysis and calcium uptake by fragmented sarcoplasmic membranes |
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| Authors: | G Inesi S Watanabe |
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| Affiliation: | 1. School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, PR China;2. Changsha Research Institute of Mining and Metallurgy Co. Ltd., Changsha 410012, PR China;1. Institute of Polymers, Composites and Biomaterials, National Research Council of Italy, via Campi Flegrei, 34, Olivetti Buildings, 80078 Pozzuoli, NA, Italy;2. Institute of Biosciences and Bio Resources, National Research Council of Italy, via P. Castellino 111, 80131 Naples, NA, Italy;3. Hematology, Department of Clinical and Molecular Medicine, Sapienza University of Rome, Via di Grottarossa, n. 1035, 00189 Rome, Italy;1. Defence Institute of Physiology and Allied Sciences (DIPAS), DRDO, Timarpur, 110054, Delhi, India;2. Department of Biochemistry, Panjab University, sector 25, Chandigarh, India |
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| Abstract: | A similar temperature dependence has been found for the initial rates of calcium uptake and ATP hydrolysis by fragmented sarcoplasmic membranes prepared from rabbit skeletal muscle. The addition of oxalate to the reaction mixture changed the temperature dependence of both calcium uptake and ATP splitting. Calcium-independent (“basal”) ATP hydrolysis displayed a temperature dependence different from that of calcium-dependent (“extra”) ATP splitting. Indirect evidence is shown to indicate that a considerable amount of calcium is bound to the membrane (40–50 μmoles/gm protein). This amount constitutes a significant portion of the total calcium taken up in the absence of oxalate, but it is negligible in comparison to the larger amount transported inside the vesicles in the presence of oxalate. |
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